Part 2

Figure: Anatomy of a hexapod insect, note that insects have a developed digestive system
(yellow), a respiratory system (blue), a circulatory system (red), and a nervous system (red).
 2.3.4 Reproduction in Frog

The common frog (Rana temoraria) is the most common in

Europe.
The grass frog genus Ptychadena goulenger is found
throughout sub-Saharan Africa, including Ethiopia.
Frogs such as Ptychadena harenna and Leptopelis ragazzi
are found in the Bale Mountains and Shoa forests, Ethiopia.
Frogs undergo sexual reproduction and have male and
female reproductive structures.
The following figure shows the male and female
reproductive structures in frogs.
 CONT…
• Unlike birds, Frogs have external fertilization, However, internal fertilization also
occurs in a few species of frogs.
• The females releases eggs from her body into the water and the male releases his
sperm to fertilize the eggs.
• The jelly-like substance in frogs protect them from drying out the eggs.
• Also frogs do not produce amniotic eggs like birds.
• Usually, frogs lay a large number of eggs in the same place at the same time.
• After fertilization of the egg, frogs go through a larval stage that is very different
from the adult form in a process called metamorphosis.
• The larval stage is called a tadpole that is different from the adult frog.
 2.3.5 Reproduction in Crocodiles
 Crocodilians are large semi-aquatic reptiles that live in different
parts of the world.
 Crocodiles reproduce sexually involving both male and female
parents. They have internal fertilization.
 The mating season for crocodiles usually begins in July or August
and mating takes place under water.
 During mating, the sperm fertilizes the egg and develops in the
female.
 The number of eggs a crocodile
deposits varies from 10 to 100,
which generally depends on the
type of species.
 Unlike frogs, crocodiles have
hard, leathery eggs that enable
them to protect their young.
 Questions
1. Which chemical substance control metamorphosis? How
2. What is the difference between Complete and incomplete
metamorphosis?
3. What is the disadvantages of external fertilization in
frogs.
4. What is the difference between a tadpole and an adult
frog?
5. What advancements or adaptations do crocodiles‟
reproductive systems have over frogs?
 2.3.6 Reproduction in Birds
 Similar to other animals, reproduction in birds enables them to produce new
individuals and perpetuate their species.
 Birds reproduce sexually and have internal fertilization. Chickens lay eggs.
Chickens are one group of birds.
 Most bird species are monogamous (have one mating partner for life).
 Monogamous is usually a mating system between a single adult male and a
single adult female for entire breeding seasons.
 But there are also polygamous species. whereas polygamous is a mating
system with several partners during a single breeding season.
 Unlike other animals, male birds do not have external genital organs whereas
females have a single ovary.
 Reproduction in birds starts by the joining of an egg or ovum with a sperm
cell in the oviduct.
 The ovum which is produced in the ovary and travels down through the
oviduct for fertilization to occur.
 The oviduct consists of the infundibulum, magnum, isthmus, uterus, and
vagina.
 Table 2.1 Parts of oviduct and functions
.
 CONT…
 Both male and female birds have a structure called the
cloaca.
 During mating, the male brings its sperm to the female
cloaca, and the sperm from the male cloaca fertilizes the
egg.
 The fertilized egg travels down to the uterus, forming a
layer of albumen around it, which is followed by the
shell membranes in the uterus.
 Then, the hard-shelled egg develops within the female
with a fluid-filled amnion, a thin membrane forming a
closed sac around the embryo.
 Birds lay eggs after the egg completes its development. The number
of eggs a bird lays varies from its species.
 Eg: penguins and albatrosses lay few eggs, but chickens and ducks
can lay more than 10 eggs.
 The structure of egg
The egg of a bird has different parts.
 The major parts of the egg of a bird are the yolk, the
chalaza, the albumen, the membranes, air sac and the
shell
 Structures of amniotic egg
Air cell: located in the large end of the egg.
Yolk: the principal nutritional source for the embryo. Albumen: clear,
cushioning protein surrounding the yolk.
Chalazae: whitish cord-like proteins that support the yolk in the center
of the albumen.
Shell membranes: there are two of these surrounding the albumin.
Shell: is composed mainly of protein embedded with calcium
carbonate. If the hen lays brown eggs, the brown pigments are added to
the shell in the last hours of shell formation. The shell contains several
thousand pores that permit the egg to "breathe
 Steps of reproduction in chickens
1.Incubation or brooding: is the process of keeping eggs warm with
body heat while the embryos inside continue to develop after birds lay
their eggs.
 In most cases, the female parent incubates the eggs, although males
sometimes participate.
 When a breeding season approaches, the female will develop a
brood patch to help transfer heat effectively.
 This brood patch has an area of skin with densely packed blood
vessels that produces more heat and facilitates heat transmission to
the egg.
 The brood patch will disappear at the end of the breeding season.
 Birds rotate their eggs periodically to ensure an even distribution of
warmth.
•This helps the embryo to finish its development inside the egg
2. Hatching: After incubation, the embryo completes its development
and hatching occurs.
 During hatching, the chick develops a tooth-like structure at the
beak‟s tip to break the egg shell.
 Moreover, the chick also communicates with its parents a day or two
before hatching, with parents with some vocal sounds.
 The chick then starts to use the hard tip of its bill, a tooth-like
structure called an egg tooth, to break out of the egg, and the young
lose the egg tooth after hatching.
Parental Care in Birds: bird use to protect
their young by building nests. Birds make
nests in areas that are hidden. Some birds do
not use nests. They simply lay their eggs on
bare camouflaged eggs. Parental Care varies
widely amongst different species of birds. In
some species, parental care ends at hatching.
Other species care for their young for an
extended time.
 2.3.7 Reproduction in rat
 Rat (genus Rattus) is the name generally applied to numerous
members of several rodent families.
 The black rat (Rattus rattus) and the brown rat (Rattus norvegicus)
are among the most common types of rats species.
 Rats live everywhere that human populations have settled.
 The black rats is predominantly live in warmer climates, and the
brown rats are dominantly found in the temperate regions.
 Giant Mole rat (Tachyoryctes macrocephalus), also known as the
giant root rat, is endemic to Ethiopia.
 Giant Mole rat is confined to high altitude shrub and grasslands in
the Afro-alpine habitat such as the Bale Mountains.
 Reproduction in rats is representative of mammalian sexual
reproduction.
 The male reproductive structure of a rat consists testes (singular
testis), scrotum seminiferous tubules, epididymis, vasdeferens and
penis with bacula.
 Similarly, the female reproductive structure of a rat consists of two
ovaries, oviducts, uterine horns and vagina with vulva.
 Pregnancy and development in rat
 Like in other mammals, rats have internal fertilization.
 The fertilized zygotes develop in the mother during a gestation period known as
pregnancy.
Pregnancy and Development
 The average pregnancy time (gestation period) of a rat varies depending on the species.
 The gestation period for a brown rat is 22 to 24 days, whereas the gestation period for
black rats is usually 22 days and the gestation period for giant mole rats is 37-49 days.
 After fertilization the formed blastula travel down the oviducts, implant in the uterine
horns, and begin to differentiate into embryonic tissue and extra- embryonic tissue.
 The umbilical cord, a complex system of connecting blood vessels nourishes the embryo
from the mother.
 The placenta transports oxygen from the mother to the embryo and removes waste from
the embryo‟s environment, and the amniotic sac protects the embryo during pregnancy.
 Gradually, the embryo forms a neural plate, which later develops into brain and spinal
cord, the arm and leg buds become visible, the nervous system pathways develop and
the rat gives birth to hairless, deaf with sealed eyelids offspring.
 Rats normally give birth from 7 to 12 offspring per litter
 After birth, the mother feeds milk and, after 45 days, the young rats are fully weaned
and are actively foraging and feeding.
 The age of sexual maturity also vary depending on species. In brown-black rats, the age
of sexual maturity is 3–4 months old. Giant mole rats become reproductively mature
when they are 4-6 months old.
. Parental care in rats: Parental
care in mammals is often
critical for the survival and
development of the offspring.
 Rats build nests to rear their
young, called pups or kittens.
The pups stay in the
nest built by their mother until
they are weaned. The female
rats care pups regardless of
which their true mothers are. If
a mother dies, the other
females will take over nursing
her pups. Male rats do not
participate in the parental care.
 Questions
1.During embryonic development, unique cell layers develop and distinguish during a stage called: A.
the blastula stage B. the germ layer stage C. the gastrula stage D. the organogenesis stage
2.Which of the following statements about insects is false? A. Insects have both dorsal and ventral
blood vessels. B. Insects have spiracles, openings that allow air to enter.
B. The trachea is part of the digestive system D. Insects have a developed digestive system with a
mouth, crop, and intestine.
3. ____were the first animals with backbone to adapt to life on land.
A.. fishes B. Amphibians C.Birds D. mammals
4. Which of the following is not true about reptiles?
A. Reptiles lay amniotic eggs B. The are cold-blooded animal groups
C. They reproduce by external fertilization D. They lay a kind of amniotic egg
5. Which of the following is not the characteristic of mammals?
A. The have Mammary Glands B. Their fetus intimately intertwined within their mother by a
placenta C. They have Four chambered heart D. They have feathers composed of keratin protein
Write
Explain the following structures of amniotic egg:
• Air cell: located in the large end of the egg.
• Yolk: the principal nutritional source for the embryo.
• Albumen: clear, cushioning protein surrounding the yolk.
• Chalazae: whitish cord-like proteins that support the yolk in the center of the albumen.
• Shell membranes: there are two of these surrounding the albumin.
• Shell: is composed mainly of protein embedded with calcium carbonate. If the hen lays brown
 2.4 The economic importance of animals (insects)
 Insects are the most diverse animals in the world.
Insects have plenty of economic importance in the world.
They have very important benefits for human beings and the ecosystem.
They have both positive and negative impacts on our economy, our lives, and the ecosystem.
Ecosystem Services provided by Invertebrates
• Pollination- many cross pollinated plants depend on insects for pollination and fruit set. Eg Honey
bees, aid in pollination of crops.
• Seed dispersal
• Natural enemies of other pests
• Decomposition
2.4.1 Beneficial aspects of insects
A. Agriculture
 One of the major activities of agriculture is crop production.
 Regarding this, insects provide services to agriculture through pollination and
regulation of pests.
i. Pollinators: insect pollinators are flower-visiting insects that forage on flowering
plants to obtain plant-provided food (nectar, pollen).
 Insects transfer male gametes (contained in pollen) to the female gametes, resulting
in pollination.
 Many plants depend on pollination for seed and fruit production.
 An estimated 35% of crop production yielded in the world is a result of insect
pollination.
 ii. Pest regulation: Natural enemies of other pests
Predators and parasitoids that attack and feed on insect pests of plants
are used in pest control.
This type pest regulation is known as a natural biological control.
 The predators destroys harmful insects that infect both animals and
plants.
Natural biological control plays an important role in limiting potential
pest populations.
Important insects in pest regulation include mantis, lady beetles,
ground beetles, rove beetles, flower bugs, lacewings and hover flies.
Eg: Insects feed on grasshoppers and caterpillars that damage crops
include: Stagmomantis insects
• Chilomenes, a ladybird beetle, feed on aphids that damage cotton
plants and destroys scale worms that are pests of orange and lemon
trees respectively.
Blister beetle
 cont…
•Epicauta, a blister beetle, eat up masses of the eggs of locusts Insects.
•Epicauta also play a great role in feeding on unwanted weeds, creating
channels for smaller organisms water, air, and roots to travel through to
improve soil aeration.
•Their activities can enhance the nutrient cycle and physical properties of the
soil, such as soil structure and tilt, and decomposers can help in the
biochemical cycling of nutrients.
B. Food
•Many species of insects are being used as a food for people in many
countries.
•Insects have potential to become a valuable source of animal protein.
• They are widely recognized as a sustainable source of animal protein.
•There are over 1,462 recorded species of edible insects in the world.
•Most insects are consumed in Asia and Central America. Usually crickets,
grasshoppers, beetle and moth larvae and termites are eaten there.
•Being rich source of protein, grasshoppers have been eaten in many parts of
the world.
•Moreover, insects are important sources of food for many vertebrates,
including birds, amphibians, reptiles, fish and mammals.
 C. Industry
• Insects have many roles in industries for manufacturing of commercial products.
• Insects are used to produce different materials at home and in industries. The following
are some of the examples.
Production of Honey and Bee Wax: Honey and wax production are considered some of
the commercial benefits of insects.
 For example, the honeybees (Apis meliffera L.) produce millions of tons of honey and
wax every year around the world.
Production of Silk: The other commercially beneficial insects are silk worms (Bombyx
mori and other silk worms).
 Silkworms produce silk fibers, which are woven into the delicate, smooth material used
for luxurious textiles and for different purposes in the textile industry.
Production of shellac: Shellac is a resin secreted by Lac insects. Among the many
species of lac insects, Laccifer lacca, is the commercially cultured lac insect.
 Shellac is still in use as dyes, inks, polishes, sealing waxes, and as stiffening agents in
the fabrication of felt hats.
 Shellac is an animal originated commercial resin.
 Production of Cochineal: Cochineal pigment (red dye) is extracted from scale insects
such as Dacylopius coccus.
 The cochineal pigment was important for the intensity and permanency
Production of Tannic Acid: Tannic acid is a chemical compound used in dyeing goods
made of leather in leather industries, for tanning and in manufacturing some inks.
Tiny wasps in the family Cynipidae secrete some chemical and in response to this, the
tree produces gall tissues that contain tannic acid.
 D. Health and medicine
 Some insects have medicinal value in treating different human and animal
diseases.
 Since ancient times, insects and insect-derived products have been used as
medicinal agents in many parts of the world.
 For instance, honey is applied to treat burns, chronic and post- surgical
wounds.
 Bee and ant venom are used to treat joints pain.
 Recent research confirms that bee products promote healthy immune
systems, improve circulation and decrease inflammation.
 Blister beetles secrete cantharidan, which acts as a powerful protein blocker
in the human body and is effective in treating severe viral infections
because it prevents the reproduction of some viral cells.
 Researchers subsequently discovered that cantharidan reacts with genetic
material of hostile cells, and therefore may be useful in the treatment of
cancerous tumors most resistant to radiation and chemotherapy.
 Several African cultures use poultices made from ground grasshoppers as
pain relievers, especially for migraines.
 2.4.2 Harmful aspects of insects
 Although most insects are beneficial, they can also be harmful to
humans and animals.
 Some insects are pests of plants, fruits, and grains in a store.
 They feed on several parts of green plants and crops, such as leaves,
stems, buds, flowers, fruits, and seeds on fields and in stores at home
 They can damaging crops and reducing production.
 These insects include locusts, caterpillars, bugs, hoppers, aphids etc.
 Have Locusts are among the most destructive of all insect pests.
 Countries have faced threats of swarms of desert locusts.
Consequently, regional and international organizations have started to
monitor desert locust populations and launch control measures when
necessary.
 Locusts are particularly destructive in hot and dry regions when there
is a sudden increase in their numbers.
 The prevalence of food shortage has further forced them to migrate.
 They migrate in huge swarms, for several kilometers away devouring
virtually every green plant in their path.
 Cont…
 Some insects are also regarded as serious pests for stored cereal
grains.
 The most common insect pests of stored cereal grains are: Rice
Weevil (Sitophilus oryzae); Lesser Grain Borer (Rhyzopertha
dominica); Rust Red Flour Beetle: (Tribolium spp.); Sawtooth Grain
Beetle: (Oryzaephilus surinamensis); Flat Grain Beetle: (Cryptolestes
spp.).

Figure: Crops destroyed by desert locusts (left) and other insects (middle and right)
 Cont…
 Moreover, several insects serve as vectors for transmitting diseases
from one organism to another or serve as intermediate hosts for
several pathogens and transfer disease from one to another.
 For example, Anopheles mosquitoes transfer malarial parasites,
“Plasmodium,” from one person to another.
 Culex mosquitos spread filariasis and transmit filarial worms from
infected to healthy people.
 The tsetse fly, Trypanosoma gambiense, also spreads the African
sleeping sickness to the human population.
 The housefly (Musca domestica) spreads food and water-borne
diseases to human populations.
 2.5 Animal Behavior
• Animal behavior means all the ways in which animals interact with
other organisms and the physical environment.
ETHOLOGY: The study of animal behavior with emphasis on the
behavioral patterns that occur in natural environments.
• It includes the movements of animals, interaction of animals within
and with the environment and learning about their environment.
2.5.1 Types of Animal Behavior
• Animal behavior can be categorized into two main types:
1. innate or inherent behavior: Nature/innate, genes determine behavior
2. learned or acquired behavior:Nurture/ learned, Experience and
learning determine behavior
 1. Innate or inherent behavior
 Innate or inherent behavior is an inborn behavior that is determined by
genes and independent of experience and specific to a species.
Innate means „inborn‟.
Innate behavior is A behavior that is present at birth or hatching.
They don‟t have to be learned.
 There are three types of innate or inherent behavior, and these are
instinctive, reflexive, and orientative.
An instinct is a complex pattern of innate behavior.
 The following examples are instinctive behaviours in animals.
@ Web making in spiders @ Nest-building in birds
@ Swimming with dolphins and other aquatic species.
@ Opening of mouth in chicks of many bird species when their
mother returns to the nest.
@ Honeybees dance when they return to the hive after finding a
source of food.
 Cont…
Reflex action
 Reflexes the simplest innate behaviors are reflex actions.
 A reflex is a sudden, an automatic, involuntary response to
stimuli.
 It does not involve a message from the brain.
During a reflex action, messages about pain do not travel all
the way to and from the brain.
Instead, they travel only as far as the spinal cord, and the
spinal cord responds to the messages by giving orders to the
muscles.
 This allows you to respond to pain more quickly.
 The following examples are reflex behaviours in animals.
@ Touch a sharp or hot object: you pull your hand away rapidly without
even thinking about
@ blinking: when something gets too close to your eye & you close your
eyes
• Orientational behaviour
Orientation in its simplest sense means taking up a particular bearing (e.g. due
south) with respect to the current position, regardless of destination.
Taxis: is directed in relation to a given stimulus.
It is the orientation of an animal (directed either towards or away) in response to
the source of stimulus. If the orientation is towards the stimulus, it is called as a
positive taxis, and if it is away from the stimulus, it is known as a negative taxis.
Example: The movement of cockroaches away from the source of light. Kinesis is
undirected, random movement.
Kinesis: is a type of locomotory behavior in relation to the source of stimulus.
The animal responds to the variation in the intensity of the stimulus and not the
source or direction of the stimulus.
 Example: The movement of woodlice in relation to the temperature around them.

Question
• What is the difference between phototaxis,
• chemotaxis, thigmotaxis and geotaxis? Explain with
 2. Learned or acquired behavior
Learned or acquired behavior is not inherited and not determined
by genes.
It is acquired through practice or a specific experience with an
external event
It is the type of animal behavior acquired during the lifetime of
an individual.
It allows an individual organism to adapt to changes in the
environment that are modified by previous experiences.
Learned behavior develops during an animal‟s lifetime.
It is modified by experience is called trial-and-err or learning.
Examples of simple learned behavior include
Non-associative learning Habituation, sensitization
 Classical conditioning, operant conditioning, latent and insight
learning
 Habituation
 Habituation is a simple form of learning in which an animal
stops responding to a stimulus, or cue, after a period of repeated
exposure.
 It is loss of responsiveness to stimuli that convey little or no
information
 Animals learn not to respond to repeated occurrences of
stimulus
 This is a form of non-associative learning, in which the
stimulus is not linked with any punishment or reward.
 E.g. The animal learns not to respond to irrelevant stimuli such
as movements due to wind, cloud, shadows, wave action etc
 For example, you were reading a book when someone turned on
the television in the same room. At first, the sound of the
television might have been annoying. After a while, you may no
longer have it noticed. Accordingly, it mean that you have
become accustomed to the sound.
 Sensitization
 It is the opposite of habituation in that repeated
presentations of the stimulus cause an increase in
response.
 Sensitization, also referred to as reverse tolerance, is a
non-associative learning process in which repeated
administration of a stimulus results in the progressive
amplification of a response.
 It occurs when a stimulus is presented above the
tolerance threshold.
 For example, repetition of a painful stimulus may
make one more sensitive to a loud noise.
 The stimulus has to be unpleasant or aversive
 In farm animals, increased responsiveness follows a
reward or punishment (or 'reinforcement') mainly
associated with predator, food and mates
 Classical conditioning
 It is a result of associative learning in which a response already associated with one
stimulus is associated with a second stimulus to which it had no previous
connection.
 A stimulus is substituted for one that is already associated with a behavior
 Animal learns to associate the new stimulus with the reward. Arbitrary stimulus
associated with a particular outcome
 It is passive
 Classical conditioning was discovered by Ivan P. Pavlov, a Russian physiologist.
There are three stages of classical conditioning. Stages:
Stage1: Before conditioning: unconditioned stimulus (UCS) produces an
unconditioned response (UCR) in an individual, which means that a stimulus in the
environment has produced a behavior or response which is unlearned (i.e.,
unconditioned), and therefore it is a natural response which has not been taught. In
this case, no new behavior has been learned yet.
Stage 2: During conditioning: During this stage, a stimulus that produces no
response is associated with the unconditioned stimulus, due to what it is known as a
conditioned stimulus (CS). For learning to take place, the UCS must be associated
with CS on a number of occasions, or trials at this stage.
Stage 3: After conditioning. This conditioning happens once the conditioned
stimulus (CS) has been associated with the unconditioned stimulus (UCS) to create a
new conditioned response.
 A stimulus is substituted for one that is already associated with a
behavior
 Animal learns to associate the new stimulus with the reward. Arbitrary
stimulus associated with a particular outcome. It is passive
 The reward follows the stimulus
 Ivan P. Pavlov a Russian scientist introduces a new stimulus before
the usual stimulus.
 Ivan P. Pavlov performed experiments using this type of conditioning.
He knew that the sight and smell of food made hungry dogs secrete
saliva.
 Operant conditioning
 Operant conditioning is a type of associative learning in which an
animal learns to associate one of its behaviors with a reward or
punishment
 The animal must perform the behavior in response to a stimulus to
get the reward
 Unlike classical conditioning, the reward follows the behavior,
not the stimulus
• Operant conditioning is a result of associative learning in which a
bit different from classical conditioning because it does not rely on
an existing stimulus-response pair.
• It was discovered by B.F. Skinner. Based on thetheory of operant
conditioning, behavior willlikely be repeated when the organism is
reinforced (rewarded), and behavior will occur less frequently
when it is punished.
• Skinner identified three types of responses or operant behavior.
• Operant conditioning allows animals to learn behaviors to receive
a reward or avoid punishment
• Reward strengthens the correct response
• Reinforcers: Increase the probability of a behaviour being repeated,
are positive or negative make response more likely in the future
• Punisher: whether positive or negative make response less likely in
the future.
• It decreases the likelihood of a behaviour being repeated.
• Neutral operants: are responses from the environment that neither
increase nor decrease the probability of a behavior being repeated.
 D. Insight learning : Problem Solving
 Highest form of learning (does not result from immediate
trial-and-error learning)
 Based on advanced perceptual abilities such as thought and
reasoning from information previously learned
 Insight learning is problem solving without trial and error
 It is sudden problem solving without prior experience
 It may involve mentally manipulating concepts to arrive at a
solution
 Problem solving is the process of devising a strategy to
overcome an obstacle
 For example, chimpanzees can stack boxes in order to reach
suspended food
 It is the ability to do something right the first time with no
prior experience
 It requires reasoning ability–the skill to look at a problem
and come up with an appropriate solution
 Insight is the most complex kind of learning
 Animal uses previous experience to respond to new situation
 E.g.: Solving math problems
Figure: Chimpanzees may use insight to solve problems.

Latent or exploratory learning

Animals explore new surroundings and learn information which
may be useful at a later stage (hence latent)
 Previous experience of playing with boxes (latent learning)
helped a Chimpazee to stack boxes and reach out to bananas at
the ceiling (Kohlar‟s work on chimpanzees).
 This response appeared to follow a period of „apparent thought‟
 Some animals learn to solve problems by observing other
individuals.
 For example, young chimpanzees learn to crack palm nuts with stones by
copying older chimpanzees
 Imprinting
Imprinting is innate behavior that is learned during a critical period early
in life of the animals
 It has both learning and innate components

Examples: Robins learn only songs of adult robins

 Birds imprint only on their “parent” during the sensitive period in their
development
 Seemingly innate behavior can be modified by experience
 Example: Herring gull chicks come to recognize own parents as they mature
 Some animals form a social attachment to the first object they see after
birth
 Activity: Table: Comparison between two types of
behaviour
No Inherited (innate) Learned behavior
behavior
1. Set at birth Acquired after animal is born

2. Species Individual characteristic behavior

characteristic
behaviour
3. Largely influenced Largely influenced by environment
by genes (inborn)

4. Inflexible Flexible
(stereotype patterns
of behaviour)
 2.5.2 Patterns of Behavior
There are different behavioral patterns in animals.
The behavioral patterns are different due to the diversity
of species.
There are also common patterns of behavior exhibited by
many species.
Examples of behavioral patterns in animals include:
Behavioral cycles  Reproductive behavior
 Social behavior  Competition
Territory and communication.
Behavioral cycles or biological clocks
Behavioral cycles are pattern in which animals respond to
periodic changes in the environment.
i. Daily or Circadian rhythms:(sleep and wake)
Circadian rhythms, are 24-hour cycles that are part of the body‟s
internal clock, running in the background to carry out essential
functions and processes.
One of the most important and well-known circadian rhythms is the
sleep-wake cycle.
Location of the clock
– Suprachiasmatic nucleus of the
hypothalamus
– Pineal gland- Secretes Melatonin
promotes sleepfulness
ii. Circalunar (circamonthly) Cycles
A circalunar cycle is about 29 days long (one lunar month).
Because the position of the moon and sun generate tidal
patterns, they can affect marine organisms
 iii. Circaannual Cycles or seasonal cycles.
A circaannual cycle is about 365 days long (one year)
For example seasonal migration (movement).
Seasonal migration refers to the movement of various
species of birds, insects, and mammals from one
habitat to another during different times of the year
because of seasonal fluctuations in factors such as the
availability of food, sunlight, temperature, and
breeding difficulty.
Example: migration of various whale and bird species
from their summer habitats in the Arctic or Antarctic
to the tropical waters near the equator and warmer
latitudes, respectively.
 Social behaviour
Social behaviour: it is the behavioral pattern of animals
commonly observed in that live in groups.
Insects such as ants, termites, bees, exhibit some of the
most well developed social behavior and wasps are social
behaviors.
One benefit of social behavior for these insects is that
different individuals perform better in certain activities or
division of labor as workers and soldiers.
Other examples
• of social behaviour are observed in elephants, penguins,
• human beings and other primates
 Eusociality

Certain social animals (such as ants and honey bees,

bumble bees) in which sterile individuals work
cooperatively with reproductive individuals that bear
the young.
• The three main features of eusociality
There is co-operation in carrying for the young
 There are usually several generations in the colony
There is division of labour
 Cont…
There are three different types of castes of bee in the colony.
I. The queen: The only reproductive fertile/female: They provided a food
called royal jell.
Role: Lay eggs, control the behaviour of the workers by releasing pheromones
II. workers: non-reproductive/ infertile females
Role: build and clean nest, forage honey by collecting nectars, take care of
the larva, attack enemies
III. Drones: reproductive active males. Fertilized egg is diploid and develops
into females. Unfertilized eggs are haploid and develop into males
 Bees “dance” to show hive
members the way to food.
• Types of dances
i. Round dance
 Is a dance for food source
within 90m (near to hive),
it doesn‟t indicate direction
i. Waggle dance
 For food source at distant >90m
 It is about distance and direction
relative to the hive and position
of the sun.
 Is a side to side wiggle of the
abdomen.
• The position is oriented Uv
light from the sun.
 Reproductive Behaviour
Reproductive behaviour: it is a behavioral pattern of animals to meet
the needs of reproduction.
It involves behaviour patterns associated with courtship, copulation,
birth, maternal care and with suckling attempts of newborn. It is
species specific behaviour.
•What is Courtship behavior?
•Courtship: is an activity that precedes and results in mating and
reproduction.
Courtship behavior: actions males and females carry out before
mating
Importance
Insures that members of the same species find each other and mate
It is vital for locating and selecting suitable mates,
Prevent interbreeding between different species
May protect male from being eaten long enough to mate
Reproductive behavior producing offspring, and rearing them
successfully.
 What controls Courtship behavior?
A. It involves chemicals/pheromones
Types of pheromones:
I. Release pheromones: Highly volatile and can attract mate from a distance of two miles or more
II. Sex hormones: pheromone release to signal the availability of a female for mate.
III. Alarm pheromones: secreted for enemies, or during attack
IV. Territorial pheromones: used to mark boundaries of a territory by the owner
• Example: Ethiopian wolves mark their territory with urine.
B. Displaying courtship rituals
It is used to strengthen already established pair bonds
C. Courtship Songs
Using vocalization to attract different sex
•Example: Songs of frogs heard on spring night and the song of humpback whale under the seas
D. Tactile- touching
 Example: Monkeys will groom each other, wolves will greet dominant males with a lick, Touch by painted
turtles
Fixed action patterns in a courtship form an important part of the mating displays in some animals,
especially of birds. Example:-Courtship behaviour in Zebra fish and mallard drake birds
 Competition
Competition: it is a behavioral pattern of animals
observed during competition such as for resources.
Example of the competition includes the
competition between animals for space, territory,
water, mates and food.
Competition occurs naturally between living
organisms that coexist in the same environment.
There are two basic types of competition:
intraspecific and interspecific.
 Territoriality:

• Territoriality: it is abehavioral pattern that involves protecting

spaces by an animal from others.
• The territories of animals contain all of the resources and
conditions they need to survive.
• Many animals defend their area by using display behavior
instead of fighting.
• The behavior gives signals for other animals to stay away.
Displaying behavior is generally safer and uses less energy than
fighting.
• For example, Male dogs and lions use pheromones in their urine
to mark their territory. It means that they are signaling other
dogs or lions to stay out of their yard.
• Male gorillas use display behavior to defend their territory by
pounding on their chests and thumping the ground with their
hands, robin by displays his red breast to warn other robins to
stay away.
 2.6 Homeostasis in animals
Homeostasis: is the self-regulatory process by which animals maintain a relatively
stable internal conditions/env‟t in their bodies regardless of external condition.
Homeostasis helps animals to:
Maintain equilibrium in the internal conditions of their bodies/cells
Maintain normal condition or constant body systems to internal and external changes
Why do animals have needed to maintain stability in their body?
 Animals are directly affected by the environmental situations.
A change in the env‟t may negatively affect the physiological functions of their bodies.
 Generally, homeostasis involves four component: stimulus, receptor, control
center, and effector
i. Stimulus: is a change in the environment that forces the organism to response.
 It is detected by receptors in the animals‟ bodies.
Example: increase or decrease in body temperature, glucose, or water.
ii. Receptor: It detect the change in the environment or body condition and send signal
to control center to counteract it, returning the internal condition to the normal.
Example: Thermoreceptors (the end of sensory neurons)
 Receptors sends information to a control center (the brain). As a result, the body
system responds to the stimulus.
 Cont…
iii. Control center: This receives messages from receptors and sends
commands to the effector to counteract the change.
 The processes of coordination occur in the part of the brain called
hypothalamus. It is a region of the brain, is a control center for
homeostasis.
 When the temperature of the environment changes (decreases or
increases), signals are sent to the brain to alert the hypothalamus.
 The hypothalamus then responds by activating the process of
vasodilation, vasoconstriction, shivering and sweating to maintain
the body temperature constant.
iv. Effector: is a nerve fiber that terminates on a muscle or gland and
stimulates contraction or secretion
 It acts on the stimulus based on the command control center,
counteracting the change and returning the internal body condition
to normal.
 The response is produced in organs or tissues such as the kidney,
liver, or heart are effectors.
 2.6.1 Thermoregulation
Thermoregulation: is the process of maintaining the internal body temperature
constant.
Based on temperature regulation (behaviour, physiology, morphology), organisms can
be classified in to two:
1. Poikilothermic animals: having body temperature that varies with
the environment
The body temperature of these organisms is generally similar to the temperature of
the environment
Poikilothermic animals are also known as ectothermic animals, lack internal control
over their body temperature.
Adaptation:
individual organisms may burrow themselves into the ground on a hot day or cold
day to keep their bodies temperature slightly below or above the environmental
temperature.
 Some poikilothermic animals seek cooler areas/shades during the hottest time of the
day.
 Some may climb onto rocks to capture heat during the coldest time of the day.
 Some animals swim in water to cool their body.
 Some also use burrows to keep their bodies warm
 Others such as bees use group activity or stay in a hive to survive in cold seasons.
 Figure: Temperature regulation in poikilotherms

2. Homoeothermic Animals
Homoeothermic or endothermic animals are those animals that
having constant and relatively high body temperature.
They can generate internal heat to maintain a constant internal
body temperature.
Their cellular processes operate optimally even when the
environment is cold and loses heat when the environment is hot.
They use morphological, physiological and behavioral methods
of temperature regulation.
 How homoeothermic animals can retain heat?
Homoeothermic animals can retain heat in a variety of ways when
the environment is cold (to conserve the body heat).
They use their fur, fat and feathers.
For example, the arctic fox uses its fluffy tail as extra insulation
when it curls up to sleep in cold weather.
Homeothermic animals also use vasoconstriction in response to the
coldest environment.
Vasoconstriction: is the narrowing of blood vessels to the skin by
the contraction of their smooth muscles to reduce blood flow in the
peripheral blood vessels and retain heat.
Shivering: is another way of maintaining body temperature in cold.
Shivering is caused by involuntary contractions of your muscles.
Muscle contractions require energy from respiration that releases
heat to warm the body.
 Figure: Temperature regulation during cold weather by puffing up feathers in birds (left),
raising hair in human (middle) and fur in fox (right)

How homoeothermic animals can loss heat?

Homeothermic animals can loss heat in a variety of ways when the environment is
hot.
Some of the ways of losing heat in response
Vasodilation: which is the opening up of arterioles to the skin through the relaxation
of their smooth muscles and by bringing more blood and heat to the body surface to loss
heat and thereby cool their body through radiation and evaporation.
Vasodilation is the widening of blood vessels at the skin surface to increase heat loss
through the surface of the skin.
Sweating: Sweating is a liquid which is produced by the sweat glands
travels up the sweat duct and out of the sweat pore onto the skin surface.
Animals also maintain their body temperature by searching out cold or hot habitats
that allow them to alter its rate of heat loss or gain, making nests or digging burrows,
huddling with conspecifics, and in human like wearing clothes or turning on an air
conditioner as human do.
Figure: The body temperature regulation
 Mechanism of heat exchange between an
animal and its environment.
In controlling the body temperature, there are four mechanism
of heat exchange between an animal and its environment.
These are radiation, evaporation, convection and
conduction.
The body structure of animals also helps to maintain their body
temperature.
For instance, large ears in hot areas help to: lose heat and cool
their body, whereas
small ears and fur in cold areas help to minimize heat loss
and keep their body warm.
The size of the animals also affects regulation of body
temperature.
How size affects regulation of body temperature of the animals?

As animals grow in size, their inside volume increases and the outside
surface area decreases. This affects the surface-area-to-volume ratio
or the surface-to-volume ratio of animals, which consequently affects
heat loss.
The greater the surface area-to-volume ratio an animal has, the
more heat loss it will have, and the smaller the surface area- to-
volume ratio an animal has the less heat loss it will have.
The smaller the animal, the higher the surface area-to-volume ratio
it will have, so it will have the higher heat loss.
Example 1: Since the size of an elephant is high, the surface area to
volume ratio becomes smaller than the surface area to volume ratio of
a rabbit.
Example 2: On the other hand, the larger the animal, the smaller the
surface area-to-volume ratio it will have.
 The ratio of metabolism to SA
 One way to become more efficient is to divide; another way
is to develop organelles that perform specific tasks. Eg
eukaryotic cells.

SA= 6(hxw) = 6(1x1) = 6 mm2 SA= 6(hxw) = 6(2x2) =

24 mm2
V= I3(length of one side) or wxhxl V= I3 = 2x2x2= 8 mm3
• V= 1mm x1mm x1mm = 1mm3 SA/VR=24/8=3or(3:1)
• SA/VR= 6 mm2/ 1mm3= 6 or (6:1)
• From the above Figure notice that as a cell increases in size, its
surface area-to-volume ratio decreases.
.
• The surface area-to-volume ratio is the relationship between the volume of an
organism and the surface area of that organism. The surface area is the external layer
of an organism.
• The volume of a cell refers to the total amount of space in that organism. The ratio
refers to the amount of surface area per unit volume of an organism.
• The surface area that an organism has is important because body heat can be either
lost to or gained from the external environment via the body‟s surface.
• The larger the surface area of an organism has, the greater the potential rate of heat
loss or gain it will have.
 2.6.2 Osmoregulation
• Osmoregulation: refers to the control of the concentration of various
liquids within the body to maintain homeostasis.
• is a process that regulates the osmotic pressure of fluids and electrolytic
balance in organisms to maintain homeostasis.
• Osmoregulation is the process of maintaining osmotic balance (salt and
water balance) in our body.
• About 60% of the human body is composed of fluids/ water.
• Types: i. intracellular fluids (12/3) and
ii. Extracellular fluid the remaining (1/3) forms our fluid between
cells (interstitial fluid) and the blood plasma.
A disruption in the osmotic pressure can result in an imbalance in the
movement of water between them and hence alter the concentration of their
electrolytes.
• Hence, osmoregulation is important to balance osmotic pressure of fluids
and electrolytes.
• In humans and other animals, this process is brought about by
osmoreceptors, which can detect changes in osmotic pressure.
• Osmoreceptors is found in the hypothalamus, part of the brain and in the
kidneys.
 There are two major types of osmoregulation:
i. Osmoconformers: organisms that try to match the osmolality of their
body with their surroundings are called osmoconformers.
Osmoconformers: maintain the same osmotic pressure inside the
body as outside water. Examples are invertebrates like starfish,
jellyfish and lobsters.
ii. Osmoregulators: organisms that actively regulate their osmotic
pressure, independent of the surrounding environment are called
osmoregulators.
Examples are many vertebrates, including humans.
 The kidney is the main organ responsible for osmoregulation in
humans.
 The hypothalamus of the brain and Antidiuretic hormone (ADH)
secreted from pituitary gland controls osmoregulation.
 How kidney works
 When the water level in the body is high,
 the kidney releases a large amount of hypotonic urine.
 When the water level is low, it retains water and produces a low amount
of hypertonic urine.
Thus, the kidneys maintain the electrolytic balance of the body.
Question: Why does your urine sometimes become yellow and sometime
not?
If the blood is too concentrated,
The hypothalamus responds by stimulating increasing the release of the
antidiuretic hormone (ADH).
 ADH increases water reabsorption from the urine.
 DH is a messenger targets the kidneys that is released straight into the
bloodstream.
 The hypothalamus responds by stimulating thirst
 If the blood is detected to be too diluted,
 The hypothalamus decreases the ADH release,
 This allowing more water to be excreted in the urine. This mechanism is
controlled by negative feedback.
 2.6.3 Blood Sugar Regulation
• Glucose: is the main source of energy for the normal functioning of
our body systems including the brain.
• The body requires volumes of glucose in order to generate energy
during respiration.
• Hence, the body regulates blood glucose level to maintain its
concentration at constant level in order to supply energy continuously.
• Normal blood sugar levels will fluctuate throughout the day, but only
slightly.
• Blood sugar levels that are too high or too low can cause health
problems.
• Low blood sugar in our body causes hypoglycemia and high blood
sugar causes diabetes.
• Hypoglycemia: Abnormally low blood sugar usually resulting from
excessive insulin or a poor diet.
 How our body controls Blood sugar levels
•Blood glucose: is regulated by the production of the two hormones:
insulin and glucagon.
•These two hormones are produced from pancreas
•When blood glucose level is high and the glucagon level is low, more
insulin is released by the pancreas into the liver.
•Insulin promotes the conversion of glucose into glycogen so that the
excess glucose can be stored for a later use in the liver.
•When blood glucose level is low and glucagon level is high, more
glucagon is released by pancreas into the liver.
•Glucagon promotes the conversion of glycogen into glucose so that the
lack of glucose can be compensated for by the new supply of glucose.
•Glycogen is stored in the liver and converted in to glucose when the
glucose level decreases.
•Therefore, insulin lowers blood glucose levels while glucagon
raises them.
 The Blood glucose level Regulation
The most common types of diabetes are type 1, and type 2
diabetes.
Type 1 diabetes: occurs when the pancreas in our body can no
longer produce insulin. People with type 1 diabetes need to take
insulin every day to stay alive.
Type 2 diabetes: occurs when the pancreas in your body doesn‟t
make enough insulin,
or your body can‟t use it properly.
Too much insulin or oral
diabetic medication can lower
the blood sugar level, leading to
hypoglycemia.
Untreated high blood sugar from
diabetes can damage our nerves,
eyes, kidneys,
and other organs.
 What we mean by negative and positive feedback control
mechanism?
Negative feedback: Occurs when a change in a variable triggers a
response that reverses the initial change.
In other words, feedback occurs when the activation of one
component results in the deactivation of another.
A negative feedback system has three basic components. These are
sensor (receptor), control center and effector.
 Example: temperature regulation in humans, this mechanism works
by promoting either heat loss or heat gain.
 Sensor (receptor) receives  Control center (hypothalamus)blood flows to the
surface of the skin
Positive feedback: occurs when a change in a variable triggers a
response that causes more change in the same direction.
Unlike negative feedback, positive feedback occurs when the
activation of one component causes the activation of another.
 Unit Three: Enzymes
3.1. What are enzymes?
 In 1877, German physiologist Wilhe kuhne first used the term enzyme, which comes
from Greek "leavened" or "in yeast".
 Enzyme- The term enzyme is coined from the active substance (extract) that are in the
yeast (en = in, zyme = yeast).
 Enzymes are a globular protein molecules that act as biological catalysts (biocatalysts)
 They have a complex 3 dimensional shape.
 They accelerate rate of chemical reactions by lowering activation energy.
 Activation energy is the minimum amount of energy required for the reactant to be
converted to products.
 Activation energy (or Ea), is minimum energy needed to start off the reaction.
 All enzymes are proteins made up of chains of amino acids linked together by peptide
bonds.
 With the exception of a small group of catalytic RNA molecules (ribozyme), all
enzymes are proteins.
 All cells contain different enzymes depending on the type of the living cell, which
engage in tremendous biochemical activity called metabolism.
 Metabolism is the process of chemical and physical changes, including catabolism and
anabolism
 Anabolic reaction: It is the reaction to synthesize (build up new molecules or products)
and Catabolic: is decompose reaction (breaks down different products).
 Enzymatic reactions
 Enzymes act upon molecules (substrates), convert them into products of different molecules, and remain
unchanged.

Substrate: The molecule the enzyme works on (acts on) is called the substrate, and their
shapes must match.
Functional sites in the enzymes system:
A. An active site/Catalytic site:
 is a region on the surface of an enzyme to which substrates will bind and catalyses a chemical
reaction.
 It is the region on the enzyme surface that catalyzes the chemical reaction, in other words, it is the site(s)
which manipulates the substrate to help rapidity of the chemical reaction. It may be separated from the
substrate-binding site by a large or a small distant or they may be combined into one site.
B. Substrate-binding site
Substrate-binding site at which substrate specifically binds and the active site is the site that carries out the
chemical action.
C. Allosteric site
The term allosteric site means “the other site” and allostery means “a change in shape”. This indicates that
when an allosteric effector non-covalently binds at allosteric site (a site other than active and substrate
binding site), it causes a conformational change in the enzyme particularity at the active site(s) that
decreases or increases the enzyme activity.
 3.2 Properties and functions of enzymes
3.2.1 General properties of an enzyme
•The general properties of enzymes are:
Enzymes accelerate the reaction rates.
Enzymes are highly specific in their action
They neither affect the nature of products formed
 They remain chemically unchanged during the reaction
The enzyme is not used up and available to catalyse further reactions
A. The physical properties of enzymes
•The physical properties of enzymes include denaturation, solubility, colloids,
biocatalysts, precipitation, molecular weight, and enzyme activity.
•Denaturation: is the process of breaking the intra and inter-molecular non-
covalent bonds that distort the shape and active site of the enzymes.
• Enzymes are denatured by high heat (above 40ºC), alternation in the pH (too
low or too high), heavy metals and high salt concentrations, solvents and
other reagents.
•Solubility is the property of enzymes that allow them to be dissolved in water,
salt (NaCl), diluted glycerol and alcohol causing denaturation.
 Cont…

• colloidal nature The colloidal nature of enzyme is the tendency of having little or
no dialysis cross the semipermeable membrane due to the large size or high
molecular weight. (Property between solution and suspension)
• The biocatalyst property is the activity of enzymes in which very small quantities
or a small amount of enzyme is enough to convert a large quantity of substrate and
remain unchanged after the reaction.
• Or small amount, of enzyme can affect a large amount of substrate
• Enzyme precipitation is the separation of enzymes for analysis using different
aqueous or ethanol solvents.
• Molecular weights of enzymes are large protein biomolecules that hold
polypeptide chains of various amino acid sequences in enzymes having a high
molecular weight.
• Enzymatic activity is the general catalytic properties of an enzyme.
• It depends on factors such as temperature, pH, and enzyme concentration and
substrate concentration.
• Enzymes show the highest activity at optimum temperature and pH that a low
concentration of enzymes and substrates slows down the enzymatic reaction.
Physical properties of Enzymes
 B. Chemical properties of enzymes
• Enzyme chemical properties are sensitivity, regulations, specificity,
catalysis and reversibility reactions.
• Heat and PH Sensitivity:
• Enzymes are sensitive to Heat (temperatures) and PH (acidity and
basicity). They work best at optimum levels.
• Regulation: is the process of controlling the activity of enzymes by
activator and inhibitor molecules.
• Catalysis: is the process of the acceleration of a chemical reaction by
a catalyst. Enzymes are biological catalysts that possess high catalytic
efficiency.
• They can transform about 100-10,000 substrates per second.
• The reactions catalyzed by the enzymes show a 103-108 times faster
reaction rate in comparison to the non-catalyzed reactions.
• Reversibility: is the ability of enzymatic biomolecules to catalyze
various metabolic (anabolic and catabolic) reactions.
• Enzymes can catalyze biochemical reactions in both forward and
reverse directions.
 Enzyme specificity
• Specificity means: The quality of being specific rather than
general
• Enzyme specificity is a property of the enzyme that
describes how restrictive the enzyme is in its choice of
substrate.
 Types of specificity of enzymes
• Bond specificity is a relative specificity of enzymes, which
indicates that enzymes are specific for a bond.
• Group specificity is a structural specificity of enzymes, which
describes that enzymes are specific for a group.
• Substrate specificity is the feature of enzymatic activity where
a particular substrate.
• A completely specific enzyme would have only one substrate.
• Absolute/compelete specificity - the enzyme will catalyze only
one reaction.
• Optical specificity is when enzymes act on the substrate optical
configuration.
• Co-factor specificity is the enzymatic specificity to the
substrate and co-factors.
• Linkage specificity - the enzyme will act on a particular type
of chemical bond regardless of the rest of the molecular
structure.
 Figure : Chemical properties of enzymes

.
 Functions of enzymes in the human body
• Enzymes help speed up chemical reactions in the human body.
• Each cell in the human body contains thousands of enzymes that
provide help in facilitating chemical reactions within each cell.
• They are essential for respiration, digesting food, the liver, muscle,
and nerve function.
• Enzymes are also used as markers of the states of various diseases like
-myocardial infraction (The middle muscular layer of the heart wall)
-jaundice (symptom of gallstones or liver infection or anemia),
-pancreatitis (Inflammation of the pancreas)
-cancer and neurodegenerative disorders etc.
• Examples of enzymes convert macromolecules into their monomers
 Sucrase breaks down a sugar called sucrose.
 Lactase breaks down lactose, a kind of sugar found in milk products.
 Carbohydrase breaks down carbohydrates into sugars.
 Lipase breaks down fats into fatty acids.
 Protease breaks down protein into amino acids
 Table: Some of enzymes in the body and their functions
Enzyme Function
Lipases Split fats found in the blood, gastric juices, pancreatic
secretions, intestinal juices, adipose (fatty) tissues and
participate in digestions.
Amylase Amylase exists in saliva and helps in changing starches
into sugars.
Maltase Maltase exists in foods such as potatoes, pasta and beer
and saliva breaks the sugar maltose into glucose.
Trypsin Found in the small intestine, breaks proteins down into
amino acids.
Lactase Found in the small intestine, breaks lactose, the sugar in
milk, into glucose and galactose.
Helicase Unwinds DNA
DNA Polymerase An enzyme responsible for forming new copies of DNA
in
the form of nucleic acids molecules
Breaks down the neurotransmitter acetylcholine in
Acetyl nerves and muscles
cholinesterase
 3.2.2 The function of enzymes
How do enzymes act as catalysts?
Enzymes perform their function by lowering a reaction's activation energy.
Activation energy: is the energy required to start a reaction.
The lower the activation energy, the faster a reaction happens.
The rate of a chemical reaction: is the rate at which reactants are converted into
products.
Therefore, enzymes increases turnover rate of the reaction.
Turnover rate: is the number of molecules of reactants that form enzyme-substrate
complexes with each molecules of an enzyme per second.
The turn over number of molecules is the number of substrates converted by one
enzyme molecule per second at saturated (fully occupied) active sites.
Before forming the results, the reactant must „climb an activation energy hill‟
before anything happens.
Under normal conditions, very few molecules have sufficient kinetic energy to
„climb the activation energy hill‟, so the reaction proceeds slowly.
More reactant molecules can meet this lower energy requirement and so the
reaction proceeds more quickly
Each enzyme has an active site with a unique shape that speeds up metabolism or
chemical reactions in our bodies and builds substances in all living things.
Enzymatic catalysis relies on the action of amino acid side chains arrayed in the
active center.
 Activation energy for catalyzed and unanalyzed reactions
.
 3.3 Protein structures
• Protein structure is a polymer of aminoacids joined by peptide bonds with three-dimensional
arrangements of atoms in amino acid chain molecules.
• Proteins have different structures.
• The protein complex macromolecules have four structural levels:
1. Primary structure 2. Secondary structure
3. Tertiary structure 4. Quaternary structure
1. The primary structure of proteins
• The primary structure of proteins makes up amino acid sequences based on the side-chain
substituents that differ by the chemical, physical, and structural properties.
• It is the sequence of amino acids linked together to form a polypeptide chain through peptide
bonds created during the protein biosynthesis process.
 Two amino-acids bond to form a dipeptide and water, during a condensation reaction. The
covalent bond between them is called a peptide bond.
 Proteins with fewer than 50 sequences are peptides, and proteins with longer than 50
sequences of amino acids are polypeptides.

• Humans require 20 amino acids out of which 10 amino acids are synthesized in the human
body, and the rest 10 amino acids are obtained from diets.
• Cells use 20 different standards of L-α-amino acids containing basic amino acids and acidic
• carboxyl groups for protein construction.
2. The secondary structure of proteins
• The secondary structure of a protein is a folded structure formed within a
polypeptide due to interactions between atoms of the backbone based on hydrogen
bonding and containing α-helix
• and ß-sheet types of strands.
The α – Helix
• α-helix – protein turns like a spiral – fibrous proteins (hair, nails, horns)
• The α-helix is a right-handed coiled
strand and the side-chain substituents
of amino acid groups extend to the
outside and form hydrogen bonds
with oxygen (C=O) in the strand with
the hydrogen of each (N-H) group of four amino acids to make the structure stable.
• ß-pleated sheet: ß-sheet – protein folds back on itself as in a ribbon –globular
protein
 3. The tertiary structure of proteins
• The tertiary protein structure is the three- dimensional shape of protein molecules
that bend and twist to achieve the maximum stability or the lowest energy state.
• The tertiary structure of protein is referred to as a specific mode of spatial
arrangement of the polypeptide chain. It is the structure of an enzyme.
• It is fashioned by many stabilizing forces due to the bonding interactions between the
side-chain groups of amino acids.
 30 structure is determined by interactions between R groups, rather than interactions
between backbone constituents.
 These interactions between R groups include
hydrogen bonds:between –OH, –NH2,,
ionic bonds:
hydrophobic interactions,
disulphide bonds/bridges : Covalent bonds &
van der Waals interactions.
 4. The quaternary structure of proteins
• Quaternary structure results when two or more polypeptide (multiple folded protein)
chains form one macromolecule
• It is the association of several protein chains or subunits into closely packed
arrangements with their own primary, secondary, or tertiary structures and held
together by the hydrogen bonds.
• Collagen is a fibrous protein consisting of three polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting of four polypeptides: two alpha and
two beta chains

Fig a. collagen structure

Fig b. Hemoglobin
 3.4 Enzyme substrate models
• Enzyme substrate models describing that the shapes of the active site and the
substrate complement to fit into the binding active site perfectly.
• The models suggest that the enzyme catalyzes the reaction by lowering the
activation energy. However, they differ in explaining how the substrate binds
to the active site of the enzyme
• There are two different of enzyme-substrate binding models that we will
look at in this section:
i. the lock and key model and
ii. the induced fit model.
1. Enzyme lock and key model
• Proposed in 1894 by a German biochemist named Fischer.
• The model proposes that the shapes of the substrate molecules are
complementary to that of the active site, rather like the shape of a key is
complementary to that of the lock it fits.
• States fit between the substrate and the active site of the enzyme is exact.l
• The substrat and enzyme fit exact like a key fits into a lock very precisely
• The model explains enzyme specificity
• This explains the loss of activity when enzymes denature.
92
 The Induced Fit Hypothesis
 Proposed in 1958 by Koshland.
 This model suggests that the active site and the substrate
aren‟t naturally complementary in shape, but the binding of substrate
molecules produces a conformational change in the active site.
 Substrate + enzyme, induces a change in the enzyme‟s conformation
 This allows the substrate and active site to bind fully.
 The conformational change also puts the substrate molecules under
tension, so they enter a „transition state‟ and are able to react because
of the lowered activation energy.
 Most biologists now prefer the induced-fit model over the lock and-
key model:
As it explains other properties of enzymes, such as enzyme inhibition,
 The rate of a chemical reaction is the rate at which reactants are converted into products.
 Some proteins can change their shape (conformation) Active site
moulded to a precise conformation.
 The bonds of the substrate are stretched to make reaction easier
93
(lowers activation energy).
 3.4.2 Enzymatic transition state
 The transition state is: is the intermediary state of the reaction, when the
molecule is neither a substrate or product or product.
 An enzymatic transition state is the reaction rates of elementary chemical
reactions and assumes chemical equilibrium between reactants and
activated transitions.
 Transition-state stabilization: The active site often acts as a flexible
molecular template that binds the substrate in a geometric structure
resembling the activated transition state of the molecule (see T* at the top
of the curve ).
 By stabilizing the substrate in its transition state, the enzyme greatly
increases the concentration of the reactive intermediate that can be
converted to product and, thus, accelerates the reaction.
 Where: E = Enzyme
S = Substrate, ES = Enzyme substrate
combined, ES*= Enzyme substrate
complexes , EP= Enzyme product,
E + S  ES ES*  EP  E + P

94
 3.5 Enzyme regulation
• Enzyme regulation is a control system for enzymatic activities.
• Enzyme regulation refers to the multiple mechanisms available to
control the activity of the enzymes.
• The enzymes are turned “on” or“off” depending on the organisms
need.
• It is adapting enzymatic activities by other molecules or metabolic
cells to either increase or decrease the activities.
• A regulatory enzyme is the one in a biochemical pathway through
which it responds to the presence of certain other biomolecules
and regulates the pathway activity.
• It requires an extra activation process to pass through some
modifications and functions.
• Types of enzyme regulation
i. Allosteric enzymes regulation
ii. Genetic and covalently modulated enzymes
iii. Enzyme inhibition
95
 1.Allosteric enzymes
 Allosteric enzymes: are enzymes that have additional binding sites other than
the active site or substrate binding site.
 Allosteric regulation occurs when an activator or inhibitor molecule binds at
specific regulatory site on the enzyme.
 The binding molecule is called an effector, it cab be inhibitor as well as
activator.
 The binding of the effector molecule/Allosteric regulatory cause/induces
conformational changes of the enzyme, leading to changes of catalytic
properties or reduce enzyme activity.
 Effectors lead to conformational changes in a concrete part of the enzyme that
affect the overall conformation of the active site, causing modifications in the
activity of the reaction
 Activator increases the activity of an enzyme, whereas inhibitor decrease the
activity after binding.
 Allosteric enzymes contain two binding sites:
i. Active site/catalytic site and
ii. Allosteric site/regulatory site
for binding effectors and
substrates respectively.
96
 Cont…
Thus, allosteric effector is called negative allosteric effector (or feedback inhibitor)
when the resulting conformational change decreases the enzyme activity. However,
the allosteric effector is called positive allosteric effector (or feedback activator) if the
resulting conformational change increases the enzyme activity.

Allosteric Catalytic/Substrate-binding site No substrate binding,

site No product

+Allosteric +
inhibitor Conformational substrate Substrate binding
Allosteric enzyme Change site unfit

+Allosteric + +
activator Conformational substrate Perfect binding Products
Allosteric enzyme
Change

97
 2. Genetic and covalent modification
Genetic regulation is one of the many mechanisms in which the structure of
the enzyme can be modified further by adding additional special group to
specific location.
The genetic and covalent modification modifies the protein surface and
facilitates intracellular delivery.
Genetic modification of enzymes is to improve the properties of enzymes
and gain active and inactive forms.
Covalent modulated enzymes are active and inactive forms of the enzymes
altered due to covalent modification of structures catalyzed by other
enzymes.
Covalent modifications are enzyme-catalyzed alterations of synthesized
proteins by the addition or removal of chemical groups.
Modifications can target a single type of amino acid or multiple amino acids
and will change the chemical properties of the site.
 Enzyme regulation occurs by the addition or elimination
of some molecules attaching to the enzyme protein.
 Examples: Phosphorylation: is the addition of
phosphate groups to proteins. It is the most frequent
regulatory modification mechanism in our cells
 3. Enzyme inhibition
 Enzyme inhibition: is a decrease in enzyme activity by enzyme
inhibitors.
 Enzyme inhibitors are molecule that binds to an enzyme and blocks
its activity. They decreases the efficacy of the enzyme
 There are two types of inhibitors.
i. Reversible inhibitors and
ii. irreversible inhibitors
Reversible inhibitor:
 The reversible inhibitor binds the enzyme non-covalently.
 So they can easily reversed.
 Reversible inhibitors can be competitive and uncompetitive.
Irreversible inhibitors
It is a substance that permanently blocks the action of an enzyme. 99
 1. Competitive inhibitor
The inhibitor has a structural similarity to the substrate.
 They compete with the substrate for the active site of the enzyme
So, it binds the active site (substrate-binding site) of in competition
with the substrate depending on their relative concentration.
Therefore, increasing substrate concentration or lowering inhibitor
concentration reverses enzyme inhibition.
Competitive inhibitor is a molecule that blocks the binding of the
substrate to the active site.
• Enzyme can only bind to either substrate or inhibitor at a time.

Figure: Competitive inhibition

100
 2. Noncompetitive inhibitor
 Noncompetitive inhibitor binds to enzyme at another site
than active site.
The inhibitor is not structurally similar to the substrate and
does not bind its binding site.
The inhibitor binds either free enzyme or the enzyme-
substrate complex (i.e., inhibitor does not prevent substrate
binding) but it decreases the enzyme catalytic rate.
This inhibition can not be overcomed by increasing substrate
concentration, but by special measures such as dialysis.
3. Uncompetitive inhibitor
 They binds only to the enzyme substrate complex, (the
intermediate state) but not to the free enzyme.
 Enzyme binds first to substrate then to inhibitors.
 It occurs in reactions with two or more substrates or
products and slows enzyme reactions by binding the
substrate to each other. 101
 3. Irreversible inhibitors
 The irreversible inhibitor binds the enzyme by covalent modification.
 Combine with the functional groups of the amino acids in the active site
irreversibly.
 It is of limited therapeutic use and are considered to be poisons.
 It decreases the concentration of the active enzyme and does not affect the
Vmax of the remaining unaffected enzyme molecules.
 e.g., inhibition of the cytochrome oxidase by cyanide.
Suicide inhibition
 A special class of irreversible inhibitors is the suicide inactivators. These
compounds are relatively unreactive until they bind to the active site of a
specific enzyme.
 These compounds are also called mechanism-based inactivators, because
they hijack the normal enzyme reaction mechanism to inactivate the
enzyme.
 Ireversible inhibition. Reaction of chymotrypsin with
diisopropylfluorophosphate (DIFP) irreversibly inhibits the enzyme. This
has led to the conclusion that Ser 195 is the key active-site Ser residue in
chymotrypsin.

102
 3.6 Types of enzymes
 Enzymes can be classified into various types.
 Enzyme types are based on how enzymes that bind specific molecules together to
form new molecules and enzymes that break specific molecules apart into separate
molecules.
Enzymes possess three types of names. They are:
•classical (trivial) or common(recommended)
•Enzyme structural classification
•systematic( scientific) names or basic classification
Trivial name
Trivial names were coined on the basis of the source from which an enzyme
was extracted eg. Pancreatic lipase,or for Greek/Latin name of the process
(eg. Pepsin - to digest, trypsin-to wear down).Consequently it may not be
possible to figure out the reaction from a trivial name.
Recommended name
Most commonly used enzyme names have the suffix "-ase" attached to the
substrate of the reaction (for example, glucosidase,urease, sucrase), or to a
description of the action performed (for example, lactate dehydrogenase and
adenylyl cyclase).
 3.6.1 Enzyme structural classification
 Deals with the separation of an enzyme into simple proteins (active)
and conjugated proteins (holoenzymes).
 There are two types of enzymes
i. Simple (only protein) ii. Complex or holoenzymes or conjugated proteins
 The conjugated protein is divided into two:
i. Apoenzyme (protein part): Are inactive groups
ii. cofactor (non-protein part): Are inactive groups
 Cofactor (non-protein part) can be divided into two:
 i. Prosthetic groups:
 usually small inorganic molecule or atom;
usually tightly bound to apoenzyme
 ii. Coenzyme
 large organic molecule (Vitamins)
 loosely bound to apoenzyme
 3.6.2 Basic or systematic classification of enzymes
 Enzymes are composed of six classes based on what and how they react, the types
of reactions they catalyzed, and the end suffix “ase”.
 The International Union of Biochemistry and Molecular Biology (IUBMB) have subdivided
enzymes into classes, subclasses and sub-subclasses and give every enzyme a written name
and a code digital name.
 The written name is formed of the substrate name, the coenzyme name and name of the
chemical process.
 The digital name is of four digits, the first refers to the enzyme class, the second refers to the
subclass, the third refers to the sub-subclass and the fourth refers to the name of the
individual enzyme itself.
In addition to its name an enzyme is also given a unique identification
number (ID-number). An enzyme's identification number is known as
enzyme code (E.C) or enzyme commission number.
Its Enzyme Commission number (E.C. 2.7.1.1.)
(2) denotes the class name  (transferase);
(7) denotes the subclass  (phosphotransferase);
(1) denotes a subsubclass phosphotransferase with a hydroxyl group as acceptor;
(1) denotes D -glucose as the phosphoryl group acceptor.
For many enzymes, a trivial name is more commonly used—in this case hexokinase.
According to this system there are 6 classes of enzymes.
 The six classes of enzymes
1. Oxidoreductases: Are a class of enzyme that catalyzes oxido-
reduction reactions.
E.g. oxidases, oxygenases, reductases, dehydrogenases & peroxidases.
 It catalyzes the transfer of electrons from one molecule (oxidant) to
other molecule (reductant) reactions in the following pattern:
A- + B ⇌ A + B- , where A is the oxidant and B is the reductant.
2. Transferase: Are enzymes catalyzing the transfer of a chemical group
from one compound to the other.
 They transfers functional groups like methyl from one donor
molecule to acceptor molecule. A-B + C ⇌ A + B-C
 E.g: aminotransferases, glycosyltransferases, methyltransferases,
acyltransferases, phosphotransferases (kinases)
3.Hydrolases: These are enzymes catalyzing the process of hydrolysis (breakdown of
the compound by addition of water), e.g., thiolases, amidases, ribonucleases,
deoxyribonucleases, hydrolytic deaminases, phospholipases, phosphatases,
glycosidases, esterase and peptidases. A-B + H2O ⇌ A-H + B-OH
 Cont…
4.Lyases: these are enzymes, which catalyze breakdown of substrates by mechanisms
other than hydrolysis and oxidation.
They are enzymes that cleave bonds by other means rather than hydrolysis or
are enzymes that cleave bonds by other means rather than hydrolysis or oxidation in
which two or more substrates are involved in one reaction. A-B ⇌ A = B + X-Y
5.Isomerases: these are enzymes catalyzing isomerization, e.g.,
Epimerases, e.g., UDP-Glucose  UDP-Galactose.
Cis-trans-isomerase, e.g., trans-Retinol  cis-Retinol.
 Mutase, e.g., glucose-6-phosphate  glucose-phosphate.
Aldo-keto-isomerase, Glucose-6- phosphate  Fructose-6- phosphate.
X Y Y X
A-B ⇌ A- B
6.Ligases or synthetases:
-These are enzymes catalyzing the process of ligation or binding of 2 molecules together
in the presence of ATP (synthetase),
- are enzymes that catalyze the joining of two molecules with concomitant hydrolysis of
the di-phosphate bond in ATP
e.g., Fatty acid + CoASH + ATP  Acyl-CoA + AMP + PPi.
Carboxylases are ligases.
A +B ⇌ A-B
 Cont…
Its Enzyme Commission number (E.C. 2.7.1.1.)

(2) denotes the class name  (transferase);

(7) denotes the subclass  (phosphotransferase);

(1) denotes a subsubclass phosphotransferase with a hydroxyl

group as acceptor;

(1) denotes D -glucose as the phosphoryl group acceptor.

For many enzymes, a trivial name is more commonly used—in this case
hexokinase.
According to this system there are 6 classes of enzymes.
 Systematic name
The International Union of Biochemistry and Molecular Biology (IUBMB) have
subdivided enzymes into classes, subclasses and sub-subclasses and give every
enzyme a written name and a code digital name.

The written name is formed of the substrate name, the coenzyme name and
name of the chemical process.

The digital name is of four digits, the first refers to the enzyme class, the
second refers to the subclass, the third refers to the sub-subclass and the fourth
refers to the name of the individual enzyme itself.
Example:The systematic name of the enzyme which catalyzes:

is ATP:glucose phosphotransferase, which indicates that it catalyzes the transfer

of a phosphoryl group from ATP to glucose.

In addition to its name an enzyme is also given a unique identification

number (ID-number). An enzyme's identification number is known as enzyme
code (E.C) or enzyme commission number.
 Cont…
Its Enzyme Commission number (E.C. 2.7.1.1.)

(2) denotes the class name  (transferase);

(7) denotes the subclass  (phosphotransferase);

(1) denotes a subsubclass phosphotransferase with a hydroxyl

group as acceptor;

(1) denotes D -glucose as the phosphoryl group acceptor.

For many enzymes, a trivial name is more commonly used—in this case
hexokinase.
According to this system there are 6 classes of enzymes.
 The six of Enzymes

Enzymes are classified into Six classes as follows:

1.Oxidoreductases: These are enzymes catalyzing oxidation-reduction
reactions, e.g., oxidases, oxygenases, reductases, dehydrogenases and
peroxidases. A- + B ⇌ A + B-
2.Transferases: These are enzymes catalyzing the transfer of a chemical
group from one compound to the other, e.g., aminotransferases,
glycosyltransferases, methyltransferases, acyltransferases,
phosphotransferases (kinases), transaldolases, transketolases and
sulfotransferases. A-B + C ⇌ A + B-C
3.Hydrolases: These are enzymes catalyzing the process of hydrolysis
(breakdown of the compound by addition of water), e.g., thiolases,
amidases, ribonucleases, deoxyribonucleases, hydrolytic deaminases,
phospholipases, phosphatases, glycosidases, esterase and peptidases.
A-B + H2O ⇌ A-H + B-OH
4.Lyases: these are enzymes, which catalyze breakdown of substrates by
mechanisms other than hydrolysis and oxidation. They include desulfhydrases and dehydratases
which reversibly remove or add H2S or water from substrate, An example is fumarase acting on fumaric
acid, Fumaric acid + H2O  Malic acid. Non-oxidative decarboxylases: which remove or add CO2, e.g.,
pyruvic decarboxylase, aldolases, lyases or cleavage enzymes are lyases. Phosphorylases cut the substrate
by adding phosphate, e.g., glycogen phosphorylase, e.g., (Glycogen)n + H3PO4  (Glycogen)n-1 + Glucose-
1-phoaphate. X Y
A-B ⇌ A = B + X-Y
5.Isomerases: these are enzymes catalyzing isomerization, e.g.,
Epimerases, e.g., UDP-Glucose  UDP-Galactose.
Cis-trans-isomerase, e.g., trans-Retinol  cis-Retinol.
 Mutase, e.g., glucose-6-phosphate  glucose-phosphate.
 Racemase, e.g., D-  L-Methylmalonyl-CoA.
Aldo-keto-isomerase, Glucose-6- phosphate  Fructose-6- phosphate.
X Y Y X
A -B ⇌ A- B

6.Ligases or synthetases:
-These are enzymes catalyzing the process of ligation or binding of 2
molecules together in the presence of ATP (synthetase),
e.g., Fatty acid + CoASH + ATP  Acyl-CoA + AMP + PPi.
Carboxylases are ligases.
A +B ⇌ A-B
 Structure of enzymes
Enzymes

Complex or holoenzymes (protein part

Simple (only protein)
and nonprotein part – cofactor)

Apoenzyme (protein Cofactor

part)

Prosthetic groups Coenzyme

-usually small inorganic -large organic
molecule or atom; molecule
-usually tightly bound to -loosely bound to
apoenzyme apoenzyme

113
Many enzymes require the presence of other compounds - cofactors -
before their catalytic activity can be exerted.

This entire active complex is referred to as the holoenzyme; i.e.,

apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic
group or metal-ion-activator) is called the holoenzyme.
Apoenzyme + Cofactor = Holoenzyme

.1- A coenzyme - a non-protein organic substance which is

dialyzable, thermostable and loosely attached to the protein part.
.2- A prosthetic group - an organic substance which is dialyzable and
thermostable which is firmly attached to the protein or apoenzyme
portion.
.3- A metal-ion-activator - these include K ,+Fe ,++Fe ,++Zn ,++Mg ,++
Ca
114
 Coenzymes
• Coenzymes act as group-transfer reagents
• Hydrogen, electrons, or groups of atoms can be
transferred

Coenzyme classification
(1) Metabolite coenzymes - synthesized from
common metabolites
(2) Vitamin-derived coenzymes - derivatives of
vitamins
Vitamins cannot be synthesized by mammals, but
must be obtained as nutrients 115
 Vitamin-Derived Coenzymes

• Vitamins are required for coenzyme synthesis

and must be obtained from nutrients

• Most vitamins must be enzymatically

transformed to the coenzyme

• Deficit of vitamin and as result correspondent

coenzyme results in the disease

116
 NAD+ and NADP+
• Nicotinic acid (niacin) an nicotinamide are precursor of
NAD and NADP
• Lack of niacin causes the disease pellagra

NAD and
NADP are
coenzymes
for
dehydro-
genases

117
 FAD and FMN
• Flavin adenine dinucleotide (FAD) and Flavin
mononucleotide (FMN) are derived from riboflavin (Vit B2)
• Flavin coenzymes are involved in oxidation-reduction
reactions

FMN (black), FAD (black/blue)

118
 3.7 Factors affecting enzyme action
 Enzymes work best within specific temperature and pH ranges and at optimal
conditions.
 optimal conditions: is the condition under which particular enzyme is most active and
effective.
 There are varieties of factors that affect the activity of enzymes: these are
temperature, pH. inhibitors,
activators, radiation, water,
changes in enzyme concentration,
substrate concentration,
changes in enzyme and
and end-product concentrations.

Temperature
 All the enzymes work best within the
specific ranges of optimum temperatures,
 Low or high temperature
causes an enzyme to lose its activity
and ability to bind a substrate and denatured.
 Once enzymes denatured,
they cannot be renatured.
 PH
 PH: enzymes function at optimum pH (the potential of hydrogen ions) that ranges
from too low (strong acid) to too high (too alkaline) pH.
 Substrate concentration
 Substrate concentrations: enzymes require a maximum limit of substrate
concentration to bind.
 at a low substrate concentration there are many active sites that are not
occupied. This means that the reaction rate is low.
 When more substrate molecules are added, more enzyme-substrate
complexes can be formed.
 As there are more active sites, and the rate of reaction increases.
Eventually, increasing the substrate concentration yet further will have no
effect.
 The active sites will be saturated so no more enzyme-substrate complexes
can be formed.
• 1.Radiation: damages enzyme activities by reducing in
enzymatic efficiency and creating disorders in the
macromolecules.
• 2. Water: affects the performance of enzymes’ activity beyond
its optimum level.
3. End product (Feedback) inhibition
• is a cellular control mechanism in that the end product inhibit
enzyme's activity. In feedback inhibition, the endproduct binds
to the
• allosteric site of the enzyme and change the structure of the
active site. This prevents the
• enzyme to perform its activity. Due to feedback inhibition, a
cell is able to know whether the amount of a product is
enough for its subsistence or not
• Example: The drug Tipranivir used to treat HIV blocks the
activity of a viral genome enzyme to make more copies as a
reversible inhibitor.
I.Effect of Enzyme Concentration
When every other variable remains constant the rate of a reaction
increases linearly as concentration of an enzyme increases
 3.9 Application of enzymes in industries and their benefits
• Application of enzymes is the use of enzymatic biochemical reactions for chemical conversion
process that are driving forces of great change for productivity of various industries.
• Enzyme protein catalytic activity is efficient enough (100s to 1000s) of times higher than that
of inorganic catalyst
3.9.1 Uses of enzyme application
• The application of enzymes are widely used in food, feed, textile, papermaking, leather and
detergents, pharmaceutical and other industrial productions.
• Examples:
1. Enzymes break down larger complex molecules into simpler molecules in our body where they
can be used to fuel our digestive systems and cellular respirations.
2.Most enzymes used for food industry were extracted from the internal organs of animals and
plants, but now most enzymes are obtained by microbial fermentation.
3.Enzymes cause billions of chemical reactions to happen at lightning speed inside the cells of
our body.
4.Enzymes improve the utilization of feed rate of starch, protein, and minerals and degrade the
anti-nutritional factors in animal feed, prevent animal indigestion and improve feed
digestibility.
5.In the pharmaceutical industry, enzymes are used in drugs, antibiotics, household products to
speed up chemical reactions and synthesis.
6. Enzymes are powerful tools in sustaining a clean environment in several ways.
7.Washing powders are enzymes used to break down protein, starch and fat stains on clothes
 Table: he applications and functions of enzymes
.
 3.10 Malting in Ethiopian tradition
• Malting (sprouting) is a widely applied traditional technology.
• It is the process of steeping, germinating and drying grain to convert
it into malt.
• Malting is the limited controlled germination of grains in moist air,
which results in the mobilization of amylases, proteases and other
enzymes that hydrolyze and modify the grain components and its
structure.
3.10.1 Steps of modern malting
• There are three steps to modern malting, steeping, germinating and
kilning, and these will be discussed in this section