react with water. e.g.
Cholesterol, steroid
LIPIDS
FATTY ACID – product of fat hydrolysis
LIPIDS - are organic compounds of biologic origin
and in general:
1. Insoluble in water
2. Soluble in organic solvents such as ether,
acetone, chloroform and Carbon tetrachloride
3. Contain carbon, hydrogen, oxygen, and
sometimes nitrogen and phosphorous
4. In most cases, yield fatty acid and glycerol
Structure of Fats and Oils /Triglycerides
Classification of Lipid based on Biochemical
Function
1. Energy storage lipid (triacyl glycerol)
2. Membrane lipid (phospholipid, sphingoglycolipid,
and cholesterol)
3. Emulsification lipid (bile acids)
4. Messenger lipid (steroid hormones, eicosanoid)
5. Protective coating lipid (biological wax)
Based upon whether or not saponification occurs
when a lipid is placed in basic aqueous solution, lipids
are divided into two categories:
1. Saponifiable lipid - are lipids that can be
converted into two or more molecules when
hydrolyzed. Examples: triacylglycerol,
phospholipids, sphingoglycolipids and
biological wax.
2. Non saponifiable lipid - cannot be broken
down into smaller units, since they do not
hormones, bile acids, and eicosanoids.
Classification of Fatty Acid
1. Saturated fatty acid - fatty acid
containing single bond. Examples: lauric acid,
palmitic acid, myristic acid and stearic acid
2. Unsaturated fatty acid - fatty acid that
contains double bond.
Unsaturated fatty acid made;
a. Monounsaturated - contains one
double bond; e.g. Palmitoleic acid
and oleic acid.
b. Polyunsaturated - contains two or
more double bond. e.g. linoleic acid,
linolenic acid, arachidonic acid.
Physical Properties of Fatty Acid
1. Short chain fatty acid is slightly soluble in
water
2. Long chain fatty acid is generally insoluble
in water.
3. As carbon atom increases, melting point
increases.
4. Long chain fatty saturated fatty acid is solid
at room temperature.
5. Long chain unsaturated fatty acid is liquid at
room temperature
6. Increasing degree of unsaturation,
decreases the melting point.
TRIACYLGLYCEROL - is an energy storage lipid
formed by esterification of three fatty acids:
1. Simple triacylglycerol - triester formed
from esterification of glycerol with and
three identical fatty acid molecules; e.g.
Glycerol tristearin
 2. Mixed triacyl glycerol - triester formed Categories of Phospholipid
from the esterification of glycerol with 1. Phosphoglycerides
more than one kind of fatty acid; e.g. Oleo -
palmito – stearin. a. Phosphatidylcholine (lecithin) - important in
the metabolism of fat by the liver and also
source of phosphoric acid which is needed or
the formation of new tissues.
b. Phosphatidylethanolamine (cephalins) -
important in blood clotting and also source of
phosphoric acid for the formation of new
tissues.
Saturated fats 2. Phosphosphingosides
- bad fats - can increase heart disease risk a. Sphingomyelins – present in large amount in
Monounsaturated fats brain, liver, and nerve tissues. Accumulation of
sphingomyelin results in mental retardation
- good fats and early death cause by lack of enzyme
- decrease both heart disease and breast cancer sphingomyelinase.
risk
- Help reduce the stickiness of blood platelets Niemann-Pick disease - a disease of infancy or early
and also help prevent the formation of blood childhood due to the accumulation of sphingomyelin in
clots and may also dissolve clots once they the brain, nerve and spleen.
form.
Polyunsaturated fats - both good fats and bad fats
PHOSPHOLIPIDS
- are found in all cell membrane as bilayer and
responsible for the passage of various
substance in and out of the cell
- contains fatty acid, an alcohol, a nitrogen
compound, and a phosphoric acid. GLYCOLIPIDS
- Found in all tissues in the human body
- are called cerebroside, they found in large
particularly in brain, liver, spinal tissue, and cell
amount in nerve tissues
membrane. Responsible for passage of various
- The structure is similar to sphingomyelin except
substances into and out of the cell.
that they contain often galactose in place of
choline and phosphoric acid.

Gaucher’s’ Disease

- the accumulation of glycolipid in the brain can

cause mental retardation at the age of three.
Juvenile and adult form of this disease are
characterized by the enlarged spleen and
kidneys. hemorrhaging, mild anemia and fragile
bones.
EICOSANOIDS - biologically active compounds derived
from arachidonic acid. They are extremely potent
compound with a variety of actions.
1. Prostaglandin - They are derived from arachidonic
acid which is formed from the nutritionally
essential fatty acid linolenic acid. It has been
isolated from most mammalian tissues, including The normal cholesterol level in human is 200 -220
male and female reproductive system, liver,
kidneys, pancreas, heart, lungs, brain, and
intestine. The richest source of prostaglandin is the
human seminal fluid.
blood stream and in gallstone. It aids in the
absorption of fatty acid from small intestine.
Atherosclerosis - form of arteriosclerosis,
result from the deposition of excess lipids,
primarily triglyceride and cholesterol from the
blood stream
mg/Dl, with slightly higher levels being normal for
normal individuals.
Other Steroids:

Prostaglandins have a wide range of physiological
effect:
a. Involved in the body’s defense against all forms of
change including those induced by chemical,
mechanical, physiologic, and pathologic stimuli.
1. Bile salts - oxidation product of cholesterol. It is
a primary component of bile. It helps in the
digestion of fats in our body and also helps to
absorb fat soluble vitamins like A, D, E and K
2. Sex hormone

b. Prostaglandin are involved in the cellular level in 3. Hormone of the adrenal cortex
regulating body function, including gastric acid 4. Ergosterol - when exposed to ultraviolet
secretion, contraction and relaxation of smooth radiation one of the product formed is
muscle, inflammation and vascular permeability, calciferol (vitamin D2)
body temperature and blood platelet aggregation.
Steroid Hormone
2. Prostacyclin - a potent inhibitor of platelet
- hormone that is the derivative of cholesterol
aggregation and is a powerful vasodilator.
1. Sex hormone
3. Thromboxane - have an effect opposite to that of
prostacyclin. They are potent aggregators of blood 2. Adrenocorticoid hormone
platelet and have a profound contractive effect on Sex hormone
a variety of smooth muscles.
1. Estrogen - female sex hormone
Both prostacyclin and thromboxane exert their
influence by regulating the production of Camp, 2. Androgen male sex hormone
with the thromboxane acts as inhibitor and 3. Progestin - the pregnancy hormone
prostacyclin as stimulator
Adrenocorticoid Hormone
4. Leukotriene - found in leukocytes (white blood
1. Mineralocorticoid Hormone – control the balance
cells). Various inflammatory and hypersensitivity
of Na+ and K+ in cells and body fluids
(allergy) responses are associated with elevated
levels of leukotrienes. 2. Glucocorticoid Hormone – control glucose
metabolism and counteract inflammation
STEROIDS - high molecular mass tetracyclic compound
with one or more (-OH) group. The most common WAX – is a compound produced by the reaction of a
sterol is cholesterol which are found in animal fat. fatty acid with high molecular mass alcohol. Water
Found in animal tissues in the brain and nerve tissues insoluble and nonreactive, hence waxes make
in the bloodstream and in gallstone. excellent protective coatings Examples:
Cholesterol - found in all animal tissues, 1. Beeswax - honeycomb of bee
particularly in the brain and nerve tissue in the 2. Spermaceti - sperm whale
3. Carnauba - carnauba palm
 4. Lanolin - Wool Identification of Fat
5. Chinese wax - in the cuticle leaves
1. Iodine number - the number of grams of iodine
6. Cholesterol palmitate - In blood plasma
taken up by 100 grams of fat
Physiological Importance of Wax: 2. Saponification number - represents the number of
1. It serves as a protective agent on the surface of alkali (KOH) required to neutralize the fatty acid
plants and animals. contained in one gram of fat.
2. It protects fruits from excessive loss of moisture 3. Reichert-Meissl Number - This is the amount of
0.1N alkali required to neutralize the volatile fatty
acids distilled from one gram of fat.
Fats - triacylglycerol that is solid at room temperature.
4. Acetyl number - represent the number of mg of
Oils - triacylglycerol that is liquid at room temperature KOH necessary to neutralize the acetic acid
liberated from the hydrolysis of one gram of
acetylated fat.
5. Polenske number - the number of mg KOH
FATS OILS required to neutralize the insoluble fatty acid from
5 grams of fat.
Triglycerides made up of one
Similarities glycerol molecule and three
fatty acid molecules Essential Fatty Acid - fatty acid needed for complete
nutrition of the human body from dietary sources,
Unsaturated / because it cannot be synthesized within the body.
Saturated / no one or more
C=C bonds 1. Linoleic acid
C=C bonds
2. Linolenic acid
Saturated Linoleic acid is the primary member of the
Unsaturated
Differences chains packed omega-6- fatty acid and linolenic acid is the primary
chains packed
closely member of omega-3 fatty acid. These two acids are
less closely
together needed for proper membrane structure and also serve
as a starting material for the production of several
Solids at room Liquids at biochemically active important long chain omegas-6
temp room temp and omega-acids.

Uses of Fat Importance of Essential Fatty Acids

1. Fat serve as the reserve supply of food energy for
the body
2. Fat is stored in adipose tissue and serve as
protector of the vital organs.
3. Fat in the outer layer of the body acts as heat
insulators
4. Fat acts as electrical insulator and allow rapid
propagation of nerve impulses.
5. Fats are constituents of lipoprotein, which are
found in the cell membrane, and in the
mitochondria and also serve as a means of
transporting lipids in the blood stream
1. Needed for proper membrane structure.
2. Serve as starting materials for the production
of several biochemically important longer-chain
omega-6 and omega -3 acids
Linoleic acid is the starting material for the
biosynthesis of arachidonic acid
Arachidonic acid is the major starting material for
Eicosanoid - substances that helps regulate blood
pressure, clotting and several other important body
functions.
Linolenic acid - is the starting material for the
biosynthesis of two additional omega-3 –fatty acids.
 1. Eicosanopentanoic acid hydrogen sulphate results in the formation of
“Acrolein” that is characterized physically by the
2. Docosahexamoic acid
release of the pungent smell.
These two acids are important constituents of
4. Hubl’s Test
the communication membrane of the brain and are
necessary for normal brain development. They are also - used to know the degree of unsaturation of
active in the retina of the eye. the given samples.
Omega-3 fatty acid - unsaturated fatty acid with its - When reacting with Hubl's reagent, oils
endmost double bond three carbon atoms away from resulting to a violet color of iodine is unsaturated
the methyl end. and if the color persists then the given fat or oil is
saturated.
Omega-6 fatty acid - unsaturated fatty acid with its
endmost double bond six carbon atoms away from the Linseed oil – unsaturated
methyl end Cotton seed oil - saturated
Chemical Reactions of Triacylglycerol 5. Salkowski’s Test
1. Hydrolysis- triacylglycerol or fat reacts with water - used to detect cholesterol in a solution. It is an
to produce fatty acid and glycerol important test used to detect cholesterol depending
2. Rancidity – fats develops an unpleasant odor and on the colors (distinct and clear colors) that yield
taste when allowed to stand at room temperature. from the reaction of cholesterol with concentrated
3. Hydrogenation – the addition of hydrogen to sulfuric acid.
double bond. Example vegetable can be converted
6. Libermann-Buchard’s Test
to fat by the addition of hydrogen in the presence
of catalysts in the process known as - also called acetic anhydride test - used for the
hydrogenation. detection of cholesterol. The formation of a green or
4. Saponification – heating of fat with strong base green-blue color after a few minutes is positive.
such as sodium chloride to produce glycerol and down into its basic building blocks, the amino acids
salts of fatty acid (soap)
MIDTERM LAB 1: Qualitative Test for Lipids
1. Solubility Test
Proteins
- the preliminary test which detects the presence PROTEINS - are compounds of high molecular mass
of all lipids consisting largely of chains of alpha amino acids
- lipids are readily miscible in non-polar solvents united by peptide bonds. It is a component of all
like chloroform, partially soluble in a polar solvent living cells and is synthesized by the cell to affect
like ethanol and immiscible in a polar solvent like growth. Upon hydrolysis proteins will be broken
water. down into its basic building blocks, the amino acids
2. Translucent Spot Test Functions of Protein

- a preliminary test for the lipids which can be
detected by the appearance of a translucent and
greasy spot. The lipid will form a greasy spot as
they are having a greasy texture that will
penetrate into the filter paper.
3. Acrolein test
- used to detect the presence of glycerol and fat -
the reaction between glycerol and potassium
1. Protein function in the body in building new cell,
maintenance of existing cells, and replacement of
old cells.
2. Proteins are important type of compound in the
body.
3. Valuable source of energy in the body.
4. Protein are involved in catalysis of biochemical
reactions
5. Protein are involved in the transfer of oxygen.
6. Protein s are component of hair, and nails as well
as connecting and supporting tissue.
7. Proteins are also involved in the transmission of
hereditary characteristics.
AMINO ACIDS
- are organic compounds that contains an amine and
carbonyl functional group, along with side chain
specific for each amino acid. The key element of an
amino acids is carbon, hydrogen, oxygen and
nitrogen. There are 20 known amino acids one is
not optically active, glycine.
- building blocks for protein
Amphoteric Nature of Amino Acid
Amino acids contain carbonyl (COOH) group,
which is acidic, and the amino (–NH2) group. In
solution, the carbonyl group can donate hydrogen ion
2. Neutral nonpolar amino acids – their molecules
to the amino group, forming a dipolar ion called the
zwitterions.
Amino acids can react to both acid and base
Amino acids are amphoteric compounds; they
can react with either acids or bases. When an amino
acid is places in basic solution, it forms a negative
charged ion that will migrate towards a positive
electrode. In an acid solution, the amino acid forms a
positively charged ion that will be attracted to
negatively charged electrode
Isoelectric point
- the pH at which the number of cations and anions
are equal.
- certain pH amino acids will not migrate toward
either the positive or negative electrode. A t this
pH, amino acid will be neutral, then there will be
equal number of positive and negative ions.
- At pH above isoelectric point, protein has more
negative than positive charge. At pH, below
isoelectric point, protein has more positive and
negative charges.
ESSENTIAL AMINO ACID - amino acid needed for
complete nutrition of the human body but cannot be
synthesized in the body. It includes; Arginine,
histidine, isoleucine, valine, leucine, lysine,
methionine, phenylalanine, threonine and tryptophan.
NONESSENTIAL AMINO ACIDS - amino acids that our
body can synthesize. Examples: alanine, arginine,
asparagine, aspartic acid, cysteine, glutamic acid,
glutamine, glycine, proline, and tyrosine.
Classification of Amino Acid
1. Neutral Polar Amino acids – Their molecule have
the same number of amino and carboxyl group.
And they are capable of forming hydrogen bonding
and therefore interact with water (hydrophilic)
Examples: serine, threonine, tyrosine,
asparagine, and glutamine
have the same number of amino and carbonyl
group. They interact poorly with water
(hydrophobic)
 Examples: Glycine, Alanine, Valine, Leucine,
Isoleucine, Phenylalanine, tryptophan,
methionine, cysteine, proline.
3. Acidic amino acid - their molecules have more
carbonyl group than amino group, such as,
glutamic acid and aspartic acid
4. Basic amino acid - their molecule has more amino
group such as lysine, arginine, and histidine.
PROTEIN STRUCTURE
3. Tertiary Structure of Protein – refers to the folding
1. Primary Structure – refers to the number and
and bending of the coil into specific layers of fibers;
sequence of amino acid. Each of the very large
number pf peptide and protein molecules in Tertiary structure of proteins is stabilized by:
biological organism have different sequence of a. Salt bridges
amino acids and that allows the protein to carry its - Protein fold so that positively charged side
function. chains are often located adjacent to
2. Secondary Structure of Protein - refers to the negatively charged side chains. The salt
recurring arrangement of the amino acid chain. bridge or ionic bond between the charged
functional groups helps stabilize the tertiary
A. Alpha helix – occurs when amino acids
structure.
forms a coil or spiral. The coils consist of loops b. Hydrogen bond
of amino acid held hydrogen bond between the - Folding is also stabilized by hydrogen
H and NH2 of one amino acid and the O of bonds that form between the polar
carbon C=O of the acid part of another amino hydrogen of one amino acid and a lone pair
acid. Examples; hair, wool. of electrons on another.
c. Disulfide bond
- Some proteins are cross-linked with
covalent bonds. The most common is a
disulfide bond between the sulfur atoms of
two cysteines. These (covalent bond) are
most common in extracellular proteins.
d. Hydrophobic bond
- Soluble globular proteins fold so that
hydrophobic side chains are mostly
B. B-pleated sheet – contains parallel strand of sequestered in the core of the protein.
polypeptide held together by hydrogen bond. The removal of the non-polar groups from
Example: Silk water (i.e. the hydrophobic effect) is the
primary force stabilizing tertiary structure.
4. Quartertiary structure- The highest level of protein
organization which applies to protein with more
than one poly peptide chain. It determines how
the different subunits of the protein fit an
organized whole. Examples: Hemoglobin
MIDTERM LAB 2: Qualitative Test for Proteins lead acetate under alkaline conditions to form
a brown precipitate.

Enzymes
Enzymes - are protein that acts as biological catalyst
that regulate the rate at which chemical reactions
provide energy in living organism without itself
being altered in the process.
In general enzymes are precipitated by protein
precipitant, like concentrated alcohol, ammonium
sulfate and trichloroacetic acid. In solution they are
1. Biuret Test
colloidal in nature and are non-dialyzable.
- It is positive for all the compounds that contain
more than one peptide bond like proteins, Biological Importance of Enzyme
proteoses, peptones, polypeptides, etc. 1. Enzymes are responsible for the different reactions
- A purplish violet color indicates a positive test. in living matter.
2. Ninhydrin Test
2. Speeds up the rate of chemical reactions to help
- a test for amino acids and proteins with a free -
support life.
NH2 group. When such an -NH2 group reacts
with ninhydrin, a purple-blue complex is 3. Help perform very important task like building
formed. muscles, destroying toxins and breaking down food
particles during digestion.
3. Xanthoproteic Test:
- uses a nitration reaction to determine the Nomenclature of enzymes:
presence of proteins in a solution. A. Upon the substrate they act upon: The suffix “ase”
- a change in color indicates a positive test. is added to the name of the substrate acted upon.
4. Millon’s Test Examples:
- used to detect the presence of soluble
proteins. 1. Amylase acts on starch
- A reddish-brown coloration or precipitate 2. Maltase acts on maltose
indicates the presence of tyrosine residue 3. Cellulase acts on cellulose
which occur in nearly all proteins. 4. Lipase acts on lipid
5. Sakaguchi Test 5. Urease acts on urea
- a chemical test used for detecting the presence B. Upon the reaction enhanced: The suffix “ase” is
of arginine in proteins. also added to the type of chemical reaction
- A red colored complex indicates a positive test. activated; Examples:
6. Hopkins-Cole Test 1. Oxidase for oxidation
- a chemical test used for detecting the presence 2. Hydrolase for hydrolysis
of tryptophan in proteins. 3. Transaminase for transfer of amino group
- A purple ring appears between the two layers if (transamination)
the test is positive for tryptophan. 4. Decarboxylase for removal of CO2
7. Sulfur Reaction or Lead Acetate Test (Decarboxylation)
- This test is specific for Sulphur containing 5. Hydrase or dehydrase for reversible addition or
amino acids.
removal of water
- The sulfur-containing amino acid such as
C. Enzyme whose names do not indicate the
cysteine, cysteine, and methionine reacts with
substance acted on or reaction enhanced.
 1. Pepsin (gastric juice)
2. Ptyalin (in saliva)
3. Trypsin (in pancreatic juice)
4. Rennin (the milk curding enzyme)
Classification of Enzyme
1. Oxidoreductases – enzyme that catalyze oxidation;
reduction reaction between two substrates.
The enzyme that catalyzes oxidation reactions
in the body are important because these reactions
are responsible for the production of energy. Many
of these enzymes are present in mitochondria.
Examples: Oxidases, reductase, hydroxylase,
transelectronases, dehydrogenases
2. Transferases – enzymes that catalyzes the transfer
of functional group between two substrates
Examples: transaminases, transmethylases,
transamidases, transpeptidases, transcarboxylases,
transulfatases
3. Hydrolases – enzyme that catalyze hydrolysis
reaction of carbohydrates, esters, and proteins
Examples:
a. Carbohydrase’s – enzyme that catalyze the
hydrolysis of carbohydrates
● Maltase – for hydrolysis of maltose to
glucose, occurs in the intestinal juice
● Ptyalin or salivary amylase, for hydrolysis of
starch and dextrin and maltose
● Sucrase - for hydrolysis of sucrose to fructose
and glucose: occurs in intestinal juice.
● Lactase - for hydrolysis of lactose to glucose
and galactose: occurs in intestinal juice.
● Amylopsin or pancreatic amylase – for the
hydrolysis of starch to dextrin and maltose;
pancreatic amylase occurs in the pancreatic
juice.
b.Esterase’s – enzyme that catalyze the hydrolysis
of esters into acids and alcohols
● Gastric lipase for the hydrolysis of fats to
fatty acids and glycerol
● Steapsin and pancreatic lipase for the
hydrolysis of fats to fatty acids and glycerol
● Phosphatase for the hydrolysis of phosphoric
acid esters to phosphoric acid
c. Proteases are enzyme that catalyze the
hydrolysis of protein to derived protein and
amino acids.
These are two types: proteinases and
peptidases
● Proteinases for the hydrolysis of proteins to
peptides
o Pepsin - found in gastric juice for the
hydrolysis of protein to polypeptide
o Trypsin found in pancreatic juice, for the
hydrolysis of protein to polypeptides
o Chymotrypsin found in pancreatic juice for
the hydrolysis of protein to polypeptides.
● Peptidases - for the hydrolysis of polypeptide to
amino acids
o Aminopeptidases – from intestinal juice
o Carboxypeptidase from pancreatic juice
o Nucleases – are enzyme that catalyze the
hydrolysis of nucleic acids;
o Examples: ribonuclease and
deoxyribonuclease
4. Lyases - are enzyme that catalyze the removal of
groups from substrate by means other than
hydrolysis, usually the formation of double bonds
Example is fumarase; which catalyze the change of
fumaric acid to L- maleic acid in the Krebs Cycle.
e.g. Deaminases, desulfuhydrases, dehydrases,
decarboxylase
5. Isomerases - enzyme that catalyze the
interconversion of cis-trans isomer/ or catalyze
intramolecular rearrangement. Example is alanine
racemase which catalyzes the conversion of D-
alanine to L-alanine which is the form the body can
use. Other examples are epimerase and mutase
6. Ligases or Synthases - enzyme that catalyzes the
coupling of two compounds with the breaking of
pyrophosphate bond. Example is the enzyme that
catalyze the formation of Malonyl CoA during
lipogenesis. Examples are carboxylase and
synthetase.
 Terminologies in Enzyme Chemistry
1. Substrate substance acted upon by an enzyme
Example: Starch is the substrate of amylase
2. Zymogen (proenzyme) – inactive form of an
enzyme
Pepsin - active form
Pepsinogen – inactive form
3. Activators – substances that convert the
proenzyme or zymogen (inactive form) into active
enzyme. Activators maybe inorganic substance or
organic in nature. Organic activators are called
kinases.
4. Holoenzyme - the combination of apoenzyme and
coenzyme
5. Antienzyme – substances that inhibit enzyme
activity
6. Apoenzyme – protein part of the enzyme
7. Coenzyme – non-protein part of the enzyme
Mechanism of Enzyme Action
1. Lock and key model - the substrate must fit in with A. Concentration of the substrate
the active site in order for the reaction to occur
2. Induced fit model – the active site must change its
conformation in order to accommodate the
incoming substrate.
Characteristic of Enzyme Action
1. High degree of Specificity – this means that an
enzyme will act only on a particular substance or
closely related substance. Examples; Proteoses can
act only on proteins but not on fats
Classification of Specificity
A. Absolute specificity – when the enzyme acts on
one and only one substrate Examples:
Arginase on arginine and urease on urea
B. Relative specificity – when an enzyme can act
on more than one substrate of related
structure but at different intensities.
Example:
Pancreatic lipase can hydrolyze fats with
greater rapidity but with simple esters at a
slower rate.
C. Stereochemical specificity – when an enzyme
can act on only a substance of specific
configuration.
Example: maltase can on alpha glucosidase but
not on beta glucosidase
Factors that affects Enzyme Action
B. Concentration of enzyme
C. Effect of pH
D. Effect of temperature
E. Time
F. Radiation
Activators and Inhibitors
Activators - inorganic substance that tend to
increase the activity of an enzyme Inhibitor – is
any substance that will make an enzyme less
active or render it inactive.
1. Competitive Inhibitor – inhibitor that compete
with the substrate in binding with active site
2. Non-competitive Inhibitor – inhibitor that does
not compete with the substrate in binding with
the active site.
MIDTERM LAB 4: Action of Salivary Amylase on Starch
Results noted:
It takes less time to reach achromic point at
37°C, as the enzyme is maximum active at this
temperature, while at higher and lower temperatures
more time is taken to reach the achromic point.
Conclusions:
● At the optimum temperature, the amylase will
break down starch very quickly.
● At low temperatures, the amylase will break
starch down slowly due to reduced kinetic
energy.
● At high temperatures, the amylase will break
starch down slowly or not at all due to
denaturation of the enzyme's active site.
● All enzymes are proteinaceous in nature. Wherein
at lower temperatures, the enzyme salivary
amylase is deactivated and at higher
temperatures, the enzyme is denaturated.
Therefore, more time will be taken by an enzyme
to digest the starch at lower and higher
temperature.
● At 37 °C, the enzyme is most active, hence, takes
less time to digest the starch.
● The optimum pH for the enzymatic activity of
salivary amylase ranges from 6 to 7. Above and
below this range, the reaction rate reduces as
enzymes get denaturated.
● Salivary amylase is most active at pH 6.8.
Moreover, the pH 5 is acidic and pH 8 is alkaline
therefore salivary amylase did not act in these
tubes whereas the enzyme acted in the tube with
ph 6.8 and digested the starch.
Vitamins – is an organic compound,
essential in small amounts for proper
functioning of the human body, that must
be obtained from dietary sources because
the body cannot synthesize it.
CLASSIFICATION
1. Water soluble vitamins - C, P, B
2. Fat Soluble vitamins - A, D, E, K
WATER SOLUBLE VITAMINS
1. Vitamin C - known as ascorbic acid
2. Vitamin P - Capillary-fragility factor
3. B- COMPLEX VITAMINS ARE
a. Thiamin (Vitamin B1)
b. Riboflavin (Vitamin B2)
c. Niacin (nicotinic acid,
nicotinamide, vitamin B3)
d. Pantothenic acid (vitamin B5)
e. Vitamin B6 (Pyridoxine,
Pyridoxal, Pyridoxamine)
f. Biotin (Vitamin B7)
g. Folate (folic acid, vitamin B9)
h. Vitamin B12 (Cobalamin)
FAT SOLUBLE VITAMINS
1. Vitamin E or Tocopherol - natural
antioxidant
2. Vitamin D – Antirachitic vitamins
3. Vitamin A – Antixeropthalmic factor
4. Vitamin K – Antihemorrhagic factor