QUESTIONS FOR MIDTERM EXAMINATION REVIEW ON BIOCHEMISTRY

1. Enzyme is widely used in many fields as food processing, environment, agriculture, medicine, etc.
You are requested to choose one out of the mentioned fields and discuss as well as demonstrate the
applications of enzyme, where possible.
Enzymes are protein molecules functioning as specialized catalysts for chemical reactions. Enzymes
have always been important to many fields, one of which is food science and technology because of their
ability to act as catalysts, transforming raw materials into improved food products.
Food processing enzymes are used in starch processing, meat processing, dairy industry, wine industry
and in the manufacture of pre-digested foods.
(i) Enzymes in Dairy industry

(ii) Enzymes in Bakery Technology

(iii) Enzymes in Fruit and Vegetable Processing and Juice Extraction

(iv) Enzymes in Starch processing

1 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
(v) Enzymes in Brewing

(vi) Enzymes in Meat processing

2 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
2. Coenzyme is helper molecule, and it takes an important role in enzyme catalyzed reaction. Discuss
about it.
A coenzyme is an organic non-protein compound. which binds with an enzyme to catalyze a reaction.
Coenzymes are often mostly called cofactors; however, they are chemically different. A coenzyme cannot
function singly but can be reused numerous times when it is paired with an enzyme.
Coenzymes can be classified into two groups depending on the interaction with apoenzyme. The
coenzymes of the first type-often called co-substrates are substrates in the reactions catalyzed by enzymes.
Co-substrate is changing during the reaction and dissociating from the active center. The original structure
of co-substrate is regenerating in the next reaction catalyzed by other enzymes. Therefore, co-substrates
cover mobile metabolic group between different reactions catalyzed by enzymes.
The second type of the coenzymes is called the prosthetic groups. The prosthetic group remains bonded
for the enzyme during the reaction. In some cases, the prosthetic group is covalently bound for its
apoenzyme, while in other cases it is weakly bound to the active center by numerous weak interactions.
Similarly to ionic amino acid residues of the active site, the prosthetic group must return to its original form
during the whole catalytic event or holoenzyme will not remain catalytically active.
Coenzyme, any of a number of freely diffusing organic compounds that function as cofactors with
enzymes in promoting a variety of metabolic reactions. Coenzymes participate in enzyme-mediated
catalysis in stoichiometric (mole-for-mole) amounts, are modified during the reaction, and may require
another enzyme-catalyzed reaction to restore them to their original state. Examples include nicotinamide
adenine dinucleotide (NAD), which accepts hydrogen (and gives it up in another reaction), and ATP, which
gives up phosphate groups while transferring chemical energy (and reacquires phosphate in another
reaction). Most of the B vitamins (see vitamin B complex) are coenzymes and are essential in facilitating
the transfer of atoms or groups of atoms between molecules in the formation of carbohydrates, fats, and
proteins. See also metabolism; stoichiometry.

3. Active site occupies a small part of an enzyme, but it is the place where substrate comes and
combines with. Base your understanding, clarify the structure and property of active site.
The active site is in the shape of a three-dimensional cleft that is composed of amino acids from
different residues of the primary amino acid sequence. The amino acids that play a significant role in the
binding specificity of the active site are usually not adjacent to each other in the primary structure, but form
the active site as a result of folding in creating the tertiary structure. This active site region is relatively
small compared to the rest of the enzyme. Similar to a ligand-binding site, the majority of an enzyme (non-
binding amino acid residues) exist primarily to serve as a framework to support the structure of the active

3 Vietnam National University - HCM INTERNATIONAL UNIVERSITY

By: Long P. Lieu

School of Biotechnology ‒ Department of Food Technology

site by providing correct orientation. The unique amino acids contained in an active site promote specific
interactions that are necessary for proper binding and resulting catalysis. Enzyme specificity depends on
the arrangement of atoms in the active site. Complementary shapes between enzyme and substrate(s) allow
a greater amount of weak non-covalent interactions including electrostatic forces, Van der Waals forces,
hydrogen bonding, and hydrophobic interactions. Specific amino acids also allow the formation of
hydrogen bonds. That shows the uniqueness of the microenvironment for the active site.
The properties of active sites includes:
- Hydrophobicity: The initial binding of substrate and enzyme occur through the non-covalent bond.
But, the catalytic site involves hydrophobic interaction in the attachment of a substrate with an enzyme.
Hydrophobic binding of the substrate to the active site of an enzyme increases the binding affinity.
- Flexibility: An active site shows flexibility as it can change its conformation to mediate substrates’
conversion into products.
- Reactivity: The active site of an enzyme reacts with the specific substrate. Its reactivity depends on
environmental conditions like temperature, pH, enzyme and substrate concentration, etc. The enzyme’s
active site combines with the substrate and thereby reduces the activation energy to further catalyze the
reaction.
- Net charge: The active site mainly consists of non-polar amino acid residues, which carry no charge
or zero net charge.

4. Write down six categories of enzyme. Discuss and focus on the first three groups.
There are the six major enzymatic categories includes Oxidoreductases, Transferases, Hydrolases,
Lyases, Isomerases, Ligases.
(i) Oxidoreductases: Oxidoreductase catalyze oxidation reduction reactions. Subclasses of this group
include the dehydrogenases, oxidases, oxygenases, reductases, peroxidase, and hydroxylases.
- These enzymes have two components; containing coenzymes as NAD+; NADP+; FAD; FMN.
- Including 4 sub-classes as:
* Dehydrogenase
- Catalyze the reaction that H+ from substrate is transferred to oxidized coenzymes as NAD+, NADP+,
FAD, FMN
Þ Can be found in glycolysis, CAC
- Catalyze the reverse reaction that H+ from reduced coenzymes NADH, NADPH, FADH2, FMNH2 is
transferred to substrate
Þ Can be found in synthesis reactions
Alcohol dehydrogenase
CH3CH2OH + NAD+ « CH3CHO + NADH + H+
® roles in alcoholic or beer.
Glutamate dehydrogenase
L-glutamic + H2O + NAD+ « α-ketoglutaric + NH3 + NADH + H+
® N from soil is transferred to plant, or help the process in which microbes can absorbed NH3.
* Reductase: Catalyze the reaction in which electron can transferred to oxygen, so oxygen can readily
combine with proton.
4 Ferocytochrom c + O2 + 4H+ « 4 Fericytochrom c + 2H2O
* Oxygenase: Catalyze the oxidation reactions in which oxygen can be a part of functional groups as
OH, COOH.
* Peroxydase
- Including peroxydase và catalase.
- Having coenzyme is hem.
- Catalize the oxidation reactions of organic molecules with the presence of H2O2.
Peroxydase:
Reduced substrate + H2O2 « Oxidized substrate + H2O
Catalase:
H2O2 + H2O2 « O2 + 2H2O

4 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 (ii) Transferases: Transferases catalyze reactions that involve the transfer of groups from one
molecule to another such as amino acid, carboxyl, carbonyl, methyl, phosphoryl, and acyl (RC=O) and the
enzyme names often go with trans such as transcarboxylase, transmethylase, and transaminases.
- Catalyze the reactions in which functional groups can be transferred.
- Complicated enzymes.
- Nature of coenzymes is different and depending on the functional.
- Examples: Acyltransferase; Glucosyltransferase; Aminotransferase; Phosphorylase.
(iii) Hydrolases: Hydrolases catalyze reactions in which the cleavage of bonds is accomplished by
adding water. Hydrolases include esterases, phosphatase, and peptidase.
- Catalyze the reactions of hydrolysis - Withoutcoenzyme
- Roles in digestion
- Examples:
+ Amylase: α-amylase, β-amylase, glucoamylase
+ Peptide hydrolase
+ Lipase

5. What do you know the enzyme kinetic? Write down the Michaelis-Menten equation and discuss
Vmax and KM.
* Enzyme kinetic:
Enzyme kinetics is the study of chemical reactions that are catalyzed by enzymes.
In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the
reaction are investigated.
Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role
in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might
affect the rate.
* The Michaelis-Menten equation
V = Vmax
[S ]
KM + [S ]
- Vmax, which is the maximum reaction velocity, is reached when all enzyme sites are saturated with
the substrate. This will happen when [S] >> KM, so that [S]/([S] + KM) approaches 1.
- KM is equal to the substrate concentration at which the reaction rate is half its maximum value. In
other words, if an enzyme has a small value of KM, it achieves its maximum catalytic efficiency at low
substrate concentrations. Thus, the smaller the value of KM, the more efficient is the catalyst. The value of
KM for an enzyme depends on the particular substrate. It also depends on the pH of the solution and the
temperature at which the reaction is carried out. For most enzymes KM lies between 10-1 and 10-7 M.

6. Can you recommend the enzyme source?

* Animal-Based Enzymes
Reliance on obtaining digestive enzymes from animal sources is challenging, because a majority of the
meat and other animal byproducts we consume are processed, pasteurized and/or cooked, which destroys
the natural enzymes.
From a digestive perspective, there are several important disadvantages associated with animal-based
enzyme sources. Temperature sensitivity is one of these. The human body does not generally have the same
temperature as the animal host of these enzymes, which can be destructive to the enzyme upon entering the
gastrointestinal tract.
Animal-based enzymes also function exclusively within a limited pH level range, which renders them
fairly ineffective in the gut. They become unstable in a low pH level (acidic) environment, resulting in the
enzyme being destroyed before it can perform its function. This pretty much eliminates the stomach as an
operational environment. As a result, to take in animal enzymes, they are better delivered into the body
within a protective enteric (polymer) coating capable of withstanding the stomach’s acidity. This means

5 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
that the enzymes do not become available to the body until they reach the small intestines. The most
common type of animal enzymes used for dietary supplementation are pancreatic enzymes.
* Plant-Based Enzymes
Fruits and vegetables are commonly consumed in their raw, natural form. This alleviates the
overarching issue with animal-based enzymes by preserving the integrity of the enzymes themselves.
Additionally, plant-based digestive enzymes are effective over a broad scope of pH levels. This range is
generally believed to be between 3.0 and 9.0, which is highly compatible with the human gastrointestinal
environment. As a result, plant-based enzymes are well-suited for supporting comprehensive digestive
health.
Four important enzymes often found in plants are protease, amylase, lipase and cellulose.
- Protease breaks down protein that can be present in meat, fish, poultry, eggs, cheese and nuts.
- Amylase assists your body with the breakdown and subsequent absorption of carbohydrates and
starches.
- Lipase aids the digestion of fat. When your diet includes lipase-rich foods, it eases the production
burden on the gall bladder, liver and pancreas.
- Cellulase is present in many fruits and vegetables, and it breaks down food fibers, which increases
their nutritional value to our bodies. The presence of cellulase in plant-based sources is important, because
it is not naturally present in the human body.
Fruits and vegetables are an ideal source for enzymes. They are enzyme-rich and easily consumed
without needing to be cooked or processed, ultimately preserving the full functionality of the enzymes.
* Fungal Enzymes
Fungal Enzymes have numerous uses. They are critical in the production and preparation of many food
products. One of the oldest known applications is the role of yeast in alcohol fermentation. Fungal enzymes
are commonly produced from a fungal source called Aspergillus.
One of the most popular and well known culinary fungi is the mushroom. Some mushroom species
produce enzymes, including hydrolases, esterases, and phenol oxidases. Fungi and their enzymes can also
be found in yeast spreads and certain types of cheeses, such as Camembert and blue cheeses.
Fungi can contain a variety of enzymes, such as protease, amylase, lipase, cellulase and tilactase
(supports lactose absorption). Like plant enzymes, fungal enzymes are acid stable and can survive within
the pH range of the stomach.

7. Pentose sugar is a component of nucleotide molecule, show how pentose sugar is structured by
drawing the pentose phosphate pathway.

6 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
8. What do you know about glycolysis, focus on structure of intermediates, enzymes, CO2, NADHs,
FADH2 and ATPs

7 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 Glycolysis is the metabolic pathway that converts glucose into pyruvic acid. The free energy released
in this process is used to form the high-energy molecules ATP and reduced NADH. Glycolysis is a sequence
of ten reactions catalyzed by enzymes.
Net Reaction: Glucose + 2NAD+ + 2 Pi + 2 ADP = 2 pyruvate + 2 ATP + 2 NADH + 2 H2O
* The 3 stages of Glycolysis
- Stage 1 is the investment stage. 2 mols of ATP are consumed for each mol of glucose
+ Glucose is converted to fructose-1,6-bisphosphate.
+ Glucose is trapped inside the cell and at the same time converted to an unstable form that can be
readily cleaved into 3-carbon units.
- In stage 2 fructose-1,6-bisphosphate is cleaved into 2 3- carbon units of glycerladehyde-3-phosphate.
- Stage 3 is the harvesting stage. 4 mols of ATP and 2 mols of NADH are gained from each initial mol
of glucose. This ATP is a result of substrate-level phosphorylation
Glyceraldehyde-3-phosphate is oxidized to pyruvate
* Step-wise reactions of glycolysis
- Reaction 1: Phosphorylation of glucose to glucose-6 phosphate.
+ This reaction requires energy and so it is coupled to the hydrolysis of ATP to ADP and Pi.
+ Enzyme: hexokinase. It has a low Km for glucose; thus, once glucose enters the cell, it gets
phosphorylated.
+ This step is irreversible. So the glucose gets trapped inside the cell. (Glucose transporters transport
only free glucose, not phosphorylated glucose)
- Reaction 2: Isomerization of glucose-6-phosphate to fructose 6- phosphate. The aldose sugar is
converted into the keto isoform.
+ Enzyme: phosphoglucomutase.
+ This is a reversible reaction. The fructose-6-phosphate is quickly consumed and the forward reaction
is favored.
- Reaction 3: is another kinase reaction. Phosphorylation of the hydroxyl group on C1 forming fructose-
1,6- bisphosphate.
+ Enzyme: phosphofructokinase. This allosteric enzyme regulates the pace of glycolysis.
+ Reaction is coupled to the hydrolysis of an ATP to ADP and Pi.
+ This is the second irreversible reaction of the glycolytic pathway.
- Reaction 4: fructose-1,6-bisphosphate is split into 2 3-carbon molecules, one aldehyde and one
ketone: dihyroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP).
+ Enzyme: aldolase.
- Reaction 5: DHAP and GAP are isomers of each other and can readily inter-convert by the action of
the enzyme triose-phosphate isomerase.
+ GAP is a substrate for the next step in glycolysis so all of the DHAP is eventually depleted. So, 2
molecules of GAP are formed from each molecule of glucose
+ Upto this step, 2 molecules of ATP were required for each molecule of glucose being oxidized
+ The remaining steps release enough energy to shift the balance sheet to the positive side. This part
of the glycolytic pathway is called as the payoff or harvest stage.
+ Since there are 2 GAP molecules generated from each glucose, each of the remaining reactions occur
twice for each glucose molecule being oxidized.
- Reaction 6: GAP is dehydrogenated by the enzyme glyceraldehyde 3-phosphate dehydrogenase
(GAPDH). In the process, NAD+ is reduced to NADH + H+ from NAD. Oxidation is coupled to the
phosphorylation of the C1 carbon. The product is 1,3-bisphosphoglycerate.
- Reaction 7: BPG has a mixed anhydride, a high energy bond, at C1. This high energy bond is
hydrolyzed to a carboxylic acid and the energy released is used to generate ATP from ADP. Product: 3-
phosphoglycerate. Enzyme: phosphoglycerate kinase.
- Reaction 8: The phosphate shifts from C3 to C2 to form 2-phosphoglycerate. Enzyme:
phosphoglycerate mutase.
- Reaction 9: Dehydration catalyzed by enolase (a lyase). A water molecule is removed to form
phosphoenolpyruvate which has a double bond between C2 and C3.

8 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 - Reaction 10: Enolphosphate is a high energy bond. It is hydrolyzed to form the enolic form of
pyruvate with the synthesis of ATP. The irreversible reaction is catalyzed by the enzyme pyruvate kinase.
Enol pyruvate quickly changes to keto pyruvate which is far more stable.

9. What do you know about C.A.C (Krebs cycle), focus on structure of intermediates, enzymes, CO2,
NADHs, FADH2 and ATPs
The citric acid cycle (CAC) – also known as the TCA cycle (tricarboxylic acid cycle) or the Krebs
cycle, which is a series of reactions that takes in acetyl-CoA and produces carbon dioxide, NADH, FADH2,
and ATP or GTP.
The TCA cycle plays a central role in the breakdown, or catabolism, of organic fuel molecules—i.e.,
glucose and some other sugars, fatty acids, and some amino acids. Before these rather large molecules can
enter the TCA cycle they must be degraded into a two-carbon compound called acetyl coenzyme A (acetyl
CoA). Once fed into the TCA cycle, acetyl CoA is converted into carbon dioxide and energy.
The TCA cycle consists of eight steps catalyzed by eight different enzymes.
1. Acetyl CoA reacts with the compound oxaloacetate to form citrate and to release coenzyme A (CoA-
SH).
Enzyme: Citrate synthase (E.C.2.3.3.1)
2. Citrate is rearranged to form isocitrate.
Enzyme: Aconitase (E.C.4.2.1.3)
3. Isocitrate loses a molecule of carbon dioxide and then undergoes oxidation to form alpha-
ketoglutarate.
Enzyme: Isocitrate dehydrogenase (E.C.1.1.1.42)
4. Alpha-ketoglutarate loses a molecule of carbon dioxide and is oxidized to form succinyl CoA.
Enzyme: α-ketoglutarase dehydrogenase (E.C.1.2.4.2)
5. Succinyl CoA is enzymatically converted to succinate.
Enzyme: Succinyl CoA synthetase (E.C.6.2.1.4, E.C.6.2.1.5)
6. Succinate is oxidized to fumarate.
Enzyme: Succinate dehydrogenase (E.C.1.3.5.1)
7. Fumarate is hydrated to produce malate.
Enzyme: Fumarase (E.C.4.2.1.2)
8. Malate is oxidized to oxaloacetate.
Enzyme: Malate dehydrogenase (E.C.1.1.1.37)
Each complete turn of the cycle results in the regeneration of oxaloacetate and the formation of two
molecules of carbon dioxide.
Energy is produced in a number of steps in this cycle of reactions. In step 5, one molecule of ATP is
produced. Most of the energy obtained from the TCA cycle, however, is captured by the compounds NAD+
and FAD and converted later to ATP. Energy transfers occur through the relay of electrons from one
substance to another, a process carried out through the chemical reactions known as oxidation and reduction
or redox reactions. For each turn of the TCA cycle, three molecules of NAD+ are reduced to NADH and
one molecule of FAD is reduced to FADH2. These molecules then transfer their energy to the electron
transport chain, a pathway that is part of the third stage of cellular respiration. The electron transport chain
in turn releases energy so that it can be converted to ATP through the process of oxidative phosphorylation.

10. What is metabolism and why do you need to study it? Base on your best understanding of
metabolism, summarize the key notes related to its basic roles and functions in living organisms.
Metabolism is the set of life-sustaining chemical reactions that convert nutrients into energy and the
complex finished products of cells.
There are two main reasons for studying a metabolic pathway:
+ To describe, in quantitative terms, the chemical changes catalyzed by the component enzymes of the
route.
+ To describe the various intracellular controls that govern the rate at which the pathway functions.
The three main roles of metabolism are:

9 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 + The conversion of food to energy to run cellular processes.
+ The conversion of food/fuel to building blocks for proteins, lipids, nucleic acids, and some
carbohydrates.
+ The elimination of metabolic wastes.
Basic functions of metabolism
+ To obtain energy from fuel molecules or sunlight
+ To convert nutrients into precursors of cellular components.
+ To assemble precursors utilizing energy into cellular components.

11. Show out and demonstrate for your understanding upon the key roles of carbohydrates
metabolism and the utmost important metabolic ways, of which in the Chemistry of biological
science, and especially in human health.
Carbohydrate metabolism is the various biochemical processes responsible for the formation,
breakdown and interconversion of carbohydrates in living organisms.
* Key roles of carbohydrates metabolism
- In human body, carbohydrates have crucial roles. Our body health needs carbs for energy.
Example: The foods we eat are ultimately converted into glucose, absorbed into blood and provide
energy for every activity in our body. Glucose can be stored as Glycogen in Liver and muscles.
- Since energy is primarily converted from glucose, a sufficient carbohydrate supply can help to spare
proteins.Thus, proteins will be used effectively, not be wasted as fuel.
- Fat oxidation: carbs metabolism produce oxaloacetic acid, which used for metabolizing fat in the
correct way.
- Oxaloacetic acid combines with acetyl CoA to form Citric acid.If there is no Oxaloacetic acid, acetyl
CoA would likely to form Ketone in Ketosis which is not good at high accumulation. (causing frequent
urination, stomach pain, nausea, vomiting, etc.)
Benefitting digestion: the bacteria in the GI tract consume carbohydrates, which then will produce
some vitamins the body needs. Lactate helps absorb calcium better.
Building materials: Carbs can combine with protein and lipid to make Glycoprotein and Glycolipid in
cells for special duties (e.g. Signaling).
* Carbohydrate metabolism with commonly known diseases: Hypoglycemia (low blood sugar)
symptoms, Hard wound healing, Lower rate of vitamins absorption due to lack of metabolic.
Fuel, Immunodeficiency: lacking energy and material for immunological activities,etc.
* The utmost important metabolic ways: pentose phosphate pathway (conversion of hexose sugars
into pentoses), glycogenesis (conversion of excess glucose into glycogen, stimulated by insulin),
glycogenolysis (conversion of glycogen polymers into glucose, stimulated by glucagon) and
gluconeogenesis (de novo glucose synthesis).

12. Discuss and exemplify the difference between anabolism and catabolism, where possible.
Characteristics Anabolism Catabolism
Anabolism is a set of enzyme-catalyzed Catabolism is a set of enzyme-catalyzed
reactions that synthesize relatively reactions that breakdown large complex
Definition
complex molecules from simple molecules into smaller units in living
structures in living systems. systems.
Role in Anabolism is the constructive phase of Catabolism is the destructive phase of
metabolism metabolism. metabolism.
In anabolism, large complex molecules In catabolism, large molecules are broken
Process
are synthesized from smaller molecules. down to form smaller molecules.
Anabolic reactions require a considerable Catabolic reactions release a
Energy
amount of energy. considerable amount of energy.
Anabolic reactions are endergonic Catabolic reactions are exergonic
Reaction
reactions. reactions.

10 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 Catabolic processes require oxygen as
Oxygen is not required for anabolic
Role of oxygen most of the reactions are oxidation
processes.
reactions.
Energy During anabolism, kinetic energy in the During catabolism, potential energy is
conversion body is converted to potential energy. converted into kinetic energy.
Anabolic processes usually occur when Catabolic processes usually occur when
Occurs during
the body is at rest or asleep. the body is active and requires energy.
Hormones like estrogen, testosterone, Hormones like adrenaline, cortisol,
Hormones
growth hormones, and insulin are glucagon, and cytokines are involved in
involved
involved in anabolism. catabolism.
In growing cells, anabolism dominates Catabolic reactions are less prevalent
Growing cells
over catabolism. than anabolic reactions in growing cells.
Anabolic reactions are often anaerobic in Catabolic reactions are aerobic and result
Effects on
nature and result in a build-up of muscle in burning fat and calories during
exercise
mass. exercise.
Primary Anabolism is essential for the growth and Catabolism is essential to perform
function maintenance of living systems. different activities in living systems.
Processes like photosynthesis, protein Processes like cellular respiration,
Examples biosynthesis, and assimilation are some digestion, and excretion are some
examples of anabolic processes. examples of catabolic processes.

13. Focus and discuss the energy generating pathways of carbohydrate metabolism.

14. What is Biochemistry and its covering scopes as well as its applications in life sciences? Show
your understanding and give examples, where possible.
Biochemistry, study of the chemical substances and processes that occur in plants, animals, and
microorganisms and of the changes they undergo during development and life. It deals with the chemistry
of life, and as such it draws on the techniques of analytical, organic, and physical chemistry, as well as
those of physiologists concerned with the molecular basis of vital processes. All chemical changes within
the organism—either the degradation of substances, generally to gain necessary energy, or the buildup of
complex molecules necessary for life processes—are collectively called metabolism. These chemical
changes depend on the action of organic catalysts known as enzymes, and enzymes, in turn, depend for
their existence on the genetic apparatus of the cell. It is not surprising, therefore, that biochemistry enters
into the investigation of chemical changes in disease, drug action, and other aspects of medicine, as well as
in nutrition, genetics, and agriculture.
Biochemistry has obvious applications in medicine, dentistry, and veterinary medicine. Other
applications include:
- Food Science: Biochemists determine the chemical composition of foods, research ways to develop
abundant and inexpensive sources of nutritious foods, develop methods to extract nutrients from waste
products, and/or invent ways to prolong the shelf life of food products.
- Agriculture: Biochemists study the interaction of herbicides/insecticides with plants and pests. They
examine the structure–activity relationships of compounds, determine their ability to inhibit growth, and
evaluate the toxicological effects on surrounding life.
- Pharmacology, Physiology, Microbiology, Toxicology, and Clinical Chemistry: Biochemists
investigate the mechanisms of drug actions; engage in viral research; conduct research pertaining to organ
function; or use chemical concepts, procedures, and techniques to study the diagnosis and therapy of disease
and the assessment of health.

15. Show your understanding and exemplifying, where possible, the fate of metabolic pathway.
Metabolic pathway is a step-by-step series of interconnected biochemical reactions that convert a
substrate molecule or molecules through a series of metabolic intermediates, eventually yielding a final
product or products.

11 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology
 Each metabolic pathway consists of a series of biochemical reactions that are connected by their
intermediates: the products of one reaction are the substrates for subsequent reactions, and so on. Metabolic
pathways are often considered to flow in one direction. Although all chemical reactions are technically
reversible, conditions in the cell are often such that it is thermodynamically more favorable for flux to
proceed in one direction of a reaction. For example, one pathway may be responsible for the synthesis of a
particular amino acid, but the breakdown of that amino acid may occur via a separate and distinct pathway.
One example of an exception to this "rule" is the metabolism of glucose. Glycolysis results in the
breakdown of glucose, but several reactions in the glycolysis pathway are reversible and participate in the
re-synthesis of glucose (gluconeogenesis).
- Glycolysis was the first metabolic pathway discovered:
+ As glucose enters a cell, it is immediately phosphorylated by ATP to glucose 6-phosphate in the
irreversible first step.
+ In times of excess lipid or protein energy sources, certain reactions in the glycolysis pathway may
run in reverse to produce glucose 6-phosphate, which is then used for storage as glycogen or starch.
- Metabolic pathways are often regulated by feedback inhibition.
- Some metabolic pathways flow in a 'cycle' wherein each component of the cycle is a substrate for the
subsequent reaction in the cycle, such as in the Krebs Cycle.
- Anabolic and catabolic pathways in eukaryotes often occur independently of each other, separated
either physically by compartmentalization within organelles or separated biochemically by the requirement
of different enzymes and co-factors.
+ Anabolic pathways require an input of energy to synthesize complex molecules from simpler ones.
One example of an anabolic pathway is the synthesis of sugar from CO2. Other examples include the
synthesis of large proteins from amino acid building blocks and the synthesis of new DNA strands from
nucleic acid building blocks. These processes are critical to the life of the cell, take place constantly, and
demand energy provided by ATP and other high-energy molecules like NADH and NADPH.
+ Catabolic pathways involve the degradation of complex molecules into simpler ones, releasing the
chemical energy stored in the bonds of those molecules. Some catabolic pathways can capture that energy
to produce ATP, the molecule used to power all cellular processes. Other energy-storing molecules, such
as lipids, are also broken down through similar catabolic reactions to release energy and make ATP.

12 By: Long P. Lieu

Vietnam National University - HCM INTERNATIONAL UNIVERSITY
School of Biotechnology ‒ Department of Food Technology