Biology Lesson Note For 11th Graders

Unit - 3 Enzymes (Enzymology)

By: Getaneh T.
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Unit – 3
Enzymes (Enzymology)
3.1. What are enzymes?
Active
Enzymes are globular proteins which functions site
as biological catalysts, speeding up reaction
rate by lowering activation energy without
affected by the reaction being catalysed.

- Enzymes have a uniquely shaped structure or region called the active site.
 Active site – the part of an enzyme molecule that binds with its substrate.
 Substrate - a substance upon which an enzyme acts in a biochemical reaction.
- When a substrate bind with the active site an enzyme-substrate complex can be
formed.

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• Enzymes are proteins that act as biological catalysts (biocatalysts).
- Exception – ribozymes (RNA molecules) act as non-protein biocatalysts.
• Enzymes speed up chemical reactions by lowering the activation energy.
N.B: Activation energy (Ea) is the minimum amount of energy (free) required to
start a chemical reaction (convert reactants to products).
• Enzymes are composed of chains of amino acids linked by peptide bonds.
• All living cells contain different enzymes based on their cell type and type of
reactions taken place.
• Enzymes drive metabolism, which includes; catabolism (breakdown of molecules
and anabolism (synthesis of molecules).
Metabolism = Anabolism + Catabolism
• Metabolic processes require enzymes to catalyze reactions at life-sustaining rates.
• Enzymes act on substrates to form products, and remain unchanged after the
reaction.

Exercise 1
I. Give short answer for each of the following questions.
1. What are enzymes?
2. What are the building blocks of enzymes?
3. What is the active site of an enzyme, and how does it facilitate the enzyme's
function in catalyzing reactions?
4. What is activation energy?
5. What do we call the total amount of the biochemical reactions involved in
maintaining the living condition of the cells in an organism?
6. Distinguish between anabolism and catabolism.
7. Why are there so many different types of enzymes in your body?
8. Why is a small amount of enzyme enough for catalyzing a large number of
substrate molecules into products?

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 3.2 Properties and functions of enzymes
3.2.1 General properties of an enzyme
- Enzymes are biological catalysts that accelerate reaction rates without being
consumed in the reaction.
- They do not alter the nature of products formed.
A. The physical properties of enzymes

The physical properties of enzymes include;

1. Denaturation
– Involves breaking intra- and intermolecular bonds, altering the enzyme's shape
and active site.
– Caused by; High temperature (above 40°C), extreme pH, heavy metals, high
salt concentrations, and solvents.
2. Solubility
– Enzymes dissolve in water, diluted alcohol, glycerol, or salt solutions.
3. Colloidal Nature
– Enzymes are large molecules that do not pass (dialysis) through semipermeable
membranes easily.
4. Biocatalyst Property
– Small amounts of enzymes can catalyze reactions involving large amounts of
substrates without being changed.
5. Precipitation
– Enzymes can be separated for analysis using solvents like ethanol or water.
6. Molecular Weight
– Enzymes are large protein biomolecules made of polypeptide chains, giving
them a high molecular weight.
7. Enzyme Activity
– Influenced by temperature, pH, enzyme concentration, and substrate
concentration. 6
 B. Chemical properties of enzymes

Chemical properties of enzymes include;

1. Heat and pH Sensitivity
- Enzymes function best at optimum temperature and pH, beyond which they
become less effective or denatured.
2. Regulation
- Enzymes are regulated by activators (increase activity) and inhibitors (decrease
activity).
3. Catalysis
- Enzymes accelerate reactions by factors of 10³–10⁸ compared to uncatalyzed
reactions.
- They can process 100–10,000 substrates per second.
4. Reversibility
- Enzymes can catalyze reactions in both forward (synthesis) and reverse
(decomposition) directions.
5. Specificity
- Enzymes are highly selective about the substrates they act on, showing different
types of specificity:
a. Bond specificity - acts on specific bonds.
b. Group specificity - acts on a specific group of molecules.
c. Substrate specificity - acts on one particular substrate.
d. Optical specificity - acts on substrates with a specific optical configuration.
e. Co-factor specificity - requires specific co-factors to function.
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Exercise 2
I. Give short answer for each of the following questions.
1. Describe the physical properties of enzymes.
2. Describe the chemical properties of enzymes.
3. What is denaturation in the context of enzymes and what factors can cause it?
4. What are the main factors that determine enzyme activity?
5. What type of specificity is focused on the particular substrate an enzyme can bind
and catalyze?
6. What aspect of enzyme specificity refers to the requirement for certain non-
protein molecules to assist in catalysis?
7. In the context of enzymatic reactions, what characteristic allows some enzymes
to catalyze both forward and reverse reactions?
8. How do enzymes accelerate chemical reactions?

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 3.2.2 The function of enzymes
 Functions of enzymes include:
- Accelerate chemical reactions in the body, acting as biological catalysts.
- Support digestion by breaking down food molecules for nutrient absorption.
- Regulate metabolism by facilitating energy production and cell processes.
- Lower activation energy of reactions, making them occur more efficiently.
- Assist in cellular functions, ensuring proper functioning of organs like the liver and
muscles.
- Act as biomarkers for diagnosing diseases such as heart attack, liver damage, and
cancer.

N.B: The turn over number (kcat) of an enzyme is the maximum number of
substrates converted to products by one enzyme molecule per second at
saturated (fully occupied) active sites.

 The names of most enzymes end with the suffix “ase”. E.g. amylase.
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The breaking down of sucrose into glucose and fructose by the action of sucrase.

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 Examples of enzymes

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Exercise 3
I. Write the name of an enzyme that catalyze:
1. The conversion of hydrogen peroxide into water and oxygen
2. The synthesis of ATP from ADP and inorganic phosphate (Pi)
3. The joining of DNA fragments during DNA replication and repair
4. Unwinding of DNA strands during replication and transcription
5. The phosphorylation of glucose during glycolysis
6. The breaking down of proteins at low PH
7. The hydrolysis of sucrose into glucose and fructose
8. The hydrolysis of cellulose into simple sugars
9. The removal of hydrogen atoms from a particular substrate
10. The breaking down of lipids into glycerol and fatty acids

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 Exercise 4
I. For the following questions, match the letters with the appropriate description of
the graph of the energy flow of a chemical reaction shown below.

1. Energy path of an uncatalayzed reaction______________________

2. Energy released from this reaction__________________________
3. Activation energy of a catalyzed reaction_____________________
4. Activation energy of an uncatalayzed reaction____________________
5. Energy path of a catalyzed reaction _________________________
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Exercise 5
I. Give short answer for each of the following questions.
1. What do we call the region on an enzyme where the substrate binds?
2. What role do enzymes play in chemical reactions?
3. How do enzymes affect reaction rates in biological systems?
4. What term describes the temporary association formed between an enzyme and
its specific substrate during a catalytic reaction?
5. What is the name of an enzyme that catalyze the hydrolysis of starch into
maltose?
6. What do we call the RNA molecules with a catalytic activity, involved in various
cellular activities?
7. What is the turnover number of an enzyme?
8. What happens to an enzyme after it catalyzes a reaction?

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 3.3 Protein structures
- Protein structure is a polymer of amino acids joined by peptide bonds with three-
dimensional arrangements of atoms in amino acid chain molecules.
- The protein complex macromolecules have four structural levels:
1. The primary structure of proteins
- is he linear sequence of amino acids in a polypeptide chain, which is determined
by the genes encoding the protein.
- is stabilized by peptide bonds created between amino acids.
- Proteins with fewer than 50 amino acids are called peptides, while those with
more than 50 are polypeptides.
- Humans require 20 naturally occurring amino acids (L-α-amino acids), 11 non-
essential amino acids (synthesized in the human body), and 9 essential amino
acids (obtained from diets).

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2. The secondary structure of proteins

- refers to the folding of the polypeptide chain into α-helix and ß-sheet shapes, held
together (stabilized) by hydrogen bonds.
2.1. α-helix
- is a right-handed coil (screw) with side-chain amino acids extending outward,
stabilized by hydrogen bonds between the NH group of one amino acid and the
C=O group of an adjacent amino acid in the polypeptide backbone.
2.2. β–pleated sheet
- is a sheet-like structure where polypeptide chains run side by side, held together by
hydrogen bonds between inter- and intra-strands, forming a pleated pattern.

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3. The tertiary structure of proteins

- refers to the overall three-dimensional (3D) shape of the protein, which results
from interactions between the side-chain groups of amino acids.
- The main interactions contributing to the stability and functionality of the
protein ‘s tertiary structure include;
- Hydrogen Bonds
- Ionic Bonds
- Disulfide Bridges
- Hydrophobic Interactions

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 4. The quaternary structure of proteins
- involves the assembly of two or more polypeptide chains or subunits into a
functional protein complex.
- The individual subunits (polypeptide chains) can be held together by hydrogen
bonds.
- Not all proteins have a quaternary structure; proteins such as hemoglobin (4
polypeptides) and collagen (3 polypeptides) have quaternary structures.

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 Exercise 6
I. Give short answer for each of the following questions.
1. What level of protein structure involves the sequence of amino acids?
2. What determines the primary structure of a protein?
3. What type of bond stabilize the primary structure of a protein?
4. In which levels of protein structure do alpha helix and beta pleated sheet occur?
5. What type of interaction stabilize the secondary structure of proteins?
6. How do alpha helices and beta pleated sheets differ in protein structure?
7. Which level of protein structure involves the overall 3-D shape?
8. What type of interaction stabilize the quaternary structure of proteins?
9. What type of interactions stabilize the tertiary structure of a protein?
10. How do quaternary structures differ from tertiary structures in proteins?

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3.4.1 Enzyme-substrate binding models

- There are two models of enzyme action that explain how enzymes bind to substrates
and catalyze chemical reactions: the lock and key model and the induced fit model.
1. Lock and key model of enzyme action (Fischer, 1894)
- states that the enzyme's active site has a specific shape that exactly fits (complements)
the substrate, like a key fitting into a lock.
- The substrate binds to the enzyme's active site through non-covalent interactions.
- This model emphasizes rigid specificity - only substrates with the correct shape can
bind to the enzyme's active site.
- After catalysis, the product is released, and the enzyme’s active site remains
unchanged, allowing it to be used again for subsequent reactions.

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2. Induced fit model of enzyme action (Koshland, 1958)
• states that the enzyme's active site is flexible and undergoes a conformational change
to fit the substrate upon binding.
• The binding of the substrate induces changes in the enzyme’s shape, optimizing the fit
for catalysis.
• When the substrate binds, it induces a structural change in the enzyme, forming an
enzyme-substrate complex, which lowers the activation energy of the reaction and
increase the reaction rate.
• The induced fit enhances or suppresses enzyme activity by stabilizing the transition
state.

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3.4.2 Enzymatic transition state

- is a dynamic, unstable state that occurs during a chemical reaction when a
molecule is neither a substrate nor a product.
- involves the reaction rates of elementary chemical reactions and assumes chemical
equilibrium between reactants and activated transitions.
- it describes how the chemical reactions are taking place qualitatively in the
activated enzyme-substrate complex of absolute reaction rates.
- The reactive state of substrate binding catalysis is corresponding to the maximum
reaction activated (highest Ea) and its state of transition.
E + S ⇄ ES ⇄ ES* ⇄ EP ⇄ E + P
- E = Enzyme
- S = Substrate
- ES = Enzyme substrate
combined
- ES*= Enzyme substrate
complexes
- EP= Enzyme product

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 Exercise 7
I. Give short answer for each of the following questions.
1. What is the fundamental concept behind the lock-and-key model of enzyme
binding?
2. How does induced fit model differ from the lock-and-key model in terms of
enzyme-substrate interactions?
3. What role does the active site play in enzyme binding models?
4. Which enzyme binding model suggests a rigid, pre-existing active site for
substrate binding?
5. In the induced fit model, what happens to the enzyme’s active site upon
substrate binding?
6. Which enzyme binding model better accommodates the idea of dynamic changes
in an enzyme molecule upon binding to a substrate?
7. What is enzymatic transition state?
8. How does an enzyme influence the transition state of a chemical reaction?

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3.5 Enzyme regulation (modulation)

- is a control mechanism for enzymatic activities, where enzymes are turned “on” or
“off” based on the organism’s needs.
- involves adjusting enzyme activities by other molecules or metabolic processes to
either enhance or reduce enzyme function.
Regulatory enzymes
- A regulatory enzyme is an enzyme in a biochemical system that controls the activity of
the route through responses to the presence of specific other biomolecules.
- There are two types of regulatory enzymes; allosteric enzymes and covalently
modulated enzymes.

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1. Allosteric enzymes
- are enzymes that have additional binding sites called allosteric sites (or regulatory
sites) apart from the active site.
- active site - where the substrate binds.
- allosteric site (non-active site) - where effectors (activators or inhibitors) bind.
- Effectors (activators or inhibitors) bind reversibly to the allosteric site, causing
conformational changes in the enzyme's active site and modulating its catalytic
activity.
- activators – increase the catalytic activity of enzymes.
- inhibitors – decrease the catalytic activity of enzymes.

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2. Genetic and covalent modification

a. Genetic modification of enzymes – the process of altering their DNA to improve
the enzyme properties and produce active and inactive forms.
b. Covalent (chemical) modifications – the process of altering the enzyme's
structure by adding or removing chemical groups, such as phosphates, to change
its activity.
- Covalent modulated enzymes are active and inactive forms of the enzymes altered
due to covalent modification of structures catalyzed by other enzymes.
- Phosphorylation - involves adding phosphate groups to proteins and is the most
common regulatory modification mechanism in our cells.

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 Activation by phosphorylation and dephosphorylation

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Exercise 8
I. Give short answer for each of the following questions.
1. What is the primary purpose of enzyme regulation?
2. What are regulatory enzymes?
3. Distinguish between allosteric enzymes and covalently modulated enzymes.
4. What are the binding sites of substrates and effectors in allosteric enzymes,
respectively?
5. What is phosphorylation and what is its significance in enzyme regulation?
6. How does genetic modification and covalent modification of enzymes vary?

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3. Enzyme inhibition
- Enzyme inhibition is the process of decreasing or stopping the catalytic activity of
an enzyme by enzyme inhibitors.
- There are two types of enzyme inhibition.
a. Irreversible inhibitor - permanently blocks the action of an enzyme through
covalent strong irreversible interactions.
b. Reversible inhibitor - inactivates an enzyme temporarily through non-covalent
easily reversed interactions.
- Reversible inhibitors can be competitive, non-competitive or uncompetitive.

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i. Competitive inhibitor - is an inhibitor that competes with the substrate for

binding to the active site of an enzyme.
- occupies the active site, blocking substrate binding and inhibiting the enzyme's
catalytic function.
- Competitive inhibition can be reversed by increasing substrate concentration.

ii. Non-competitive inhibitor – is an inhibitor that binds to the enzyme at the

allosteric site (the site other than the active site).
- The binding causes conformational change that reduces the effectiveness of the
active site in catalyzing reactions.
- Non-competitive inhibitors do not directly compete with the substrates but
still hinder the enzyme’s function.

iii. Uncompetitive inhibitor – is an inhibitor that binds specifically to the

enzyme substrate complex, but not to the free enzyme.
- It stabilizes the enzyme-substrate complex, preventing the release of the product
and inhibiting the overall enzymatic reaction.
- Uncompetitive enzymes are unique in that their binding is dependent on the
presence of the substrate.
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1.

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A graph that represents the effect of competitive and non-competitive inhibitors.

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4. Feedback (end product) inhibition
- is a type of negative feedback that can be used to control metabolic pathways.
- In feedback inhibition, the end product binds to the allosteric site of the enzyme
and change the structure of the active site of an enzyme.
- Due to feedback inhibition, a cell is able to know whether the amount of a product
is enough for its subsistence or not.

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Exercise 9
I. Give short answer for each of the following questions.
1. What is the difference between inhibitors and activators?
2. How does competitive inhibition affect enzyme activity?
3. How does reversible inhibition differs from irreversible inhibition?
4. What is the role of feedback inhibition in cellular processes?
5. How does uncompetitive inhibition alter the rate of enzymatic reactions?
6. How does non-competitive inhibition affect enzyme activity?
7. Describe some applications of inhibitors.
8. How does enzyme inhibition contribute to the treatment of diseases like
HIV/AIDS?

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 3.6 Types of enzymes
3.6.1 Enzyme structural classification
• Enzymes are classified into two categories based on their structure;
1. Simple enzymes - comprise only proteins (amino acid chains), active without
additional components.
2. Conjugated enzymes (holoenzymes) - composed of both protein and non-protein
components.
a. Protein part (apoenzyme) - inactive on its own. -
- requires the non-protein part to function.
b. Non-Protein part (cofactor) - essential for enzyme activity.
- Cofactors can be coenzymes or mineral (metal) ions.
i. Coenzymes - organic molecules necessary for the catalytic activity of enzymes.
- most are derived from vitamins and often bound loosely to an apoenzyme.
- E.g. NAD (derived from niacin (B3), and FAD (derived from riboflavin (B2).
ii. Mineral (metal) ions – inorganic molecules necessary for the catalytic activity of
enzymes.
- usually bound tightly to an apoenzyme
- E.g. Mg 2+, Fe2+, Zn2+, Mn+, Cu2+, etc…
N.B: Cofactors that bound very tightly to apoenzyme are called prosthetic groups. 41

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 Exercise 10
I. Give short answer for each of the following questions.
1. Define the following biological terms.
a. Holoenzyme d. Apoenzyme
b. Coenzyme e. Prosthetic group
c. Simple enzymes f. Isoenzymes
2. What is the function of a metal ion in enzyme catalysis?
3. Give examples of inorganic cofactors.
4. Give examples of coenzymes.
5. Why is the presence of a cofactor critical for some enzymes?

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3.6.2 Basic classification of enzymes (IUBMB)

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3.6.2 Basic classification of enzymes
- Based on the type of reactions that they catalyze, enzymes are classified into six
functional classes.
- The followings are the six basic classes of enzymes.
1. Oxidoreductases - catalyzes redox reactions.
- It catalyzes the transfer of electrons from one molecule (reductant) to the other
molecule (oxidant).
- Rxn example: A– + B → A + B, where A is the reductant (electron donor) and
B is the oxidant (electron acceptor).
- Examples of oxidoreductases include; hydroxylases, oxygenases…
2. Transferases - catalyze the transfer of functional groups like methyl and
phosphate from one donor molecule to acceptor molecule.
А-В + С → А + В-С
- Examples of transferases include; transaminases, kinases…
3. Hydrolases - catalyze the hydrolysis of chemical bonds.
А-В + Н2О → А-Н + В-ОН
- Examples of hydrolases include; digestive enzymes, esterase's…
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4. Lyases - catalyze the addition or removal of groups to double bonds without

hydrolysis and oxidation.
А(ХН)-В → А=Х + В-Н
- Examples of lyases include; decarboxylases, aldolases…
5. Isomerases – catalyze change of the molecular form of the substrate
(isomerization reaction).
A−B−C → B−A−C
- Examples of isomerases include; phosphohexoisomerase, triosephosphate
isomerase…
6. Ligases (synthetases) - catalyze the joining of two molecules by forming new
bonds using energy from ATP or similar phosphate.
A + B + ATP → A-B + ADP + Pi
- Examples of ligases include; carboxylases , DNA ligases...


The scientific name of amylase is EC 3.2. 1.1.
Class  sub-class  sub-sub class  serial number (specific name)
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 Exercise 11
I. Give short answer for each of the following questions.
1. Which class of enzyme is responsible for catalyzing the transfer of electrons in
redox reactions?
2. Which class of enzymes is involved in transferring functional groups between
molecules?
3. Which enzyme class is crucial for breaking down large molecules into smaller
ones through hydrolysis?
4. Which enzyme class is associated with the formation of new bonds between
molecules using ATP?
5. Which enzyme class participates in the rearrangement of atoms within a
molecule?
6. Which enzyme class is associated with the formation or cleavage of bonds
between molecules without hydrolysis or oxidation?
7. To which class of enzymes do digestive enzymes such as pepsin and amylase
belong?
8. Distinguish between endoenzymes (intracellular) and exoenzymes (extracellular)
with examples.

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3.7 Factors affecting enzyme action

- Enzymes work best at optimal conditions (the condition under which particular
enzyme is most active), an increase or decrease in the conditions of these factors
affects the functions of enzymes.
- There are varieties of factors that affect the activity of enzymes:

Question: Explain how each of the above factors affect enzymes’ activity. 48
 3.7.1 Description of factors affecting enzymatic action
1. Temperature
- Optimum temperature – specific ranges of temperature at which enzymes work
best (effectively and efficiently).
- Low temperatures – slow down enzyme activity by reducing kinetic energy, leading
to fewer enzyme-substrate collisions.
- Extreme high temperatures – denature enzymes, altering their structure and
causing loss of activity.

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2. pH (concentration of hydrogen ions)

- Enzymes work best at optimum pH range.
- Each enzyme has an optimum pH, varying with its environment (e.g., stomach
enzymes prefer too acidic conditions, while small intestine enzymes work better in
alkaline conditions).
- Extreme pH values (too acidic or too alkaline) alters enzyme structure, preventing
substrate binding.

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3. Substrate concentration s
- Increasing s increases the reaction rate by increasing collisions between enzymes
and substrates resulting in the formation of more ES complex.
- Once all enzyme active sites are occupied and saturated with substrate, the
reaction rate reaches its maximum (plateau).
- Further increases in substrate concentration do not affect the reaction rate.

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4. Enzyme concentration E

- When the substrate is abundant, increasing enzyme concentration raises the
reaction rate as each enzyme works at its maximum turnover rate.
- However, adding more enzymes does not increase the activity of individual
enzymes; their efficiency remains constant.
N.B: - Enzyme concentration affects the overall reaction rate but not the per-enzyme
activity.

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 Exercise 12
I. Give short answer for each of the following questions.
1. What are extremozymes? Provide examples of organisms that produce them.
2. What are proenzymes (zymogens), and provide examples?
3. What do we call the temperature at which enzymes work best?
4. How does too high temperature affect enzyme activity?
5. Which enzyme in the human body works best in too acidic (low pH) conditions?
6. What happens to the reaction rate when enzyme concentration increases with
abundant substrate?
7. Why does the reaction rate plateau (become constant) at high substrate
concentrations?

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3.8 Enzyme kinetics

- Enzyme kinetics is the study of the rates of enzyme-catalyzed chemical reactions.
- In enzyme kinetics, the reaction rate is measured and the effects of varying the
conditions of the reaction such as S, E, inhibitors, etc. are investigated.
- Enzyme kinetics explains how enzymes speed up biochemical reactions by lowering
activation energy, with reaction rates depending on E and S.
Michaelis-Menten models of enzyme kinetics
- explains how the rate of an enzyme-catalyzed reaction depends on enzyme and
substrate concentrations.
- It establishes the relationship between the initial reaction rate ( V1 ), substrate
concentration [S], maximum reaction rate (Vmax), and the Michaelis constant (Km ).
- Michaelis-Menten equation is given as follows:

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 Exercise 13
I. Give short answer for each of the following questions.
1. Define enzyme kinetics.
2. Which factors influence the rate of enzyme-catalyzed reactions in enzyme
kinetics?
3. Explain the Michaelis-Menten model of enzyme kinetics.
4. Write the Michaelis-Menten equation.
5. In the Michaelis-Menten equation, what does Vmax represent and what is its role
in describing enzymatic reactions?
6. What do we call the substrate concentration required to achieve half of the
maximum reaction rate (Vmax)?
7. What are the implications of low and high Km values for an enzyme's interaction
with its substrate?

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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

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3.10 Malting in Ethiopian tradition

- Malting is the process of converting cereal grains into malt through soaking,
germinating, and drying.
- Malting is a blend of art and science, with the degree of modification assessed
through visual observation, smell, and touch.
- There are three main steps of malting;
1. Steeping - the initial process of cleaning the grain and soaking it in water and air
to activate existing hydrolytic enzymes.
2. Germinating - the grain sprouts, and enzymes break down starches and proteins
to release starch reserves, forming green malt.
3. Kilning - the process of heating or drying germinated grain to stop further
germination, reduce moisture, and develop the malt’s flavor, color, and enzymatic
activity.

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 Exercise 14
I. Give short answer for each of the following questions.
1. What types of enzymes are used in detergents, and what do they do?
2. What enzymes are used in the leather industry, and what is their purpose?
3. Define malting and describe its main steps.
4. Which type of grain is most commonly used for malting?
5. What is biochemistry, and what are its main areas of study?
6. Describe the application of each of the following enzymes.
a. Pectinase in food industry
b. Beta-glucanase brewing industry
c. Papain in food industry
d. Arginase in medical industry
e. Proteases in tannery industry
f. Lipase in tannery industry
g. Alpha- and beta-amylases in malting
h. Lactase in dairy industry

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Thank You!

“Believe you can and you are halfway there!!”

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