Biochemengg QB 2010

CH2403 BIOCHEMICAL ENGINEERING
CH2403 BIOCHEMICAL ENGINEERING LTPC

3003
AIM
To impart knowledge on the role of micro organism in different types of Bio-chemical
reaction.
OBJECTIVES
 To design Bio-chemical reactors with proper knowledge on Enzyme Engineering.
UNIT I INTRODUCTION TO BIOCHEMICAL ENGINEERING 9

An overview of industrial biochemical processes with typical examples, comparing chemical and
biochemical processes, development and scope of biochemical engineering as a discipline. Industrially
important microbial strains; their classification; structure; cellular genetics; typical examples of microbial
synthesis of biologicals.
UNIT II ENZYMES AND ENZYME KINETICS 9

Enzyme used in industry medicine and food, Their classification with typical examples of industrially
important enzymes; mechanism of enzymatic reactions; michaelis-menten kinetics; enzymes inhibition;
factors affecting the reaction rates; industrial production purification and immobilization; enzyme reactors
with typical examples.
UNIT III MICROBIAL KINETICS 9

Typical growth characteristics of microbial cells; factors affecting growth; Monod model;
modeling of batch and continuous cell growth; immobilized whole cells and their characteristics; free cell
and immobilized cell reactors; typical industrial examples; transport in cells.
UNIT IV TRANSPORT IN MICROBIAL SYSTEMS 9

Newtonian and Non-Newtonian behaviour of broths; agitation and mixing; power consumption; gas/liquid
transport in cells; transfer resistances; mass transfer coefficients and their role in scaleup of equipments;
enhancement of o2 transfer; heat transfer correlation; sterilization cycles and typical examples of heat
addition and during biological production.
UNIT V BIOREACTORS 9
Batch and continuous types; immobilized whole cell and enzyme reactors; high performance bioreactors;
sterile and non-sterile operations; reactors in series with and without recycle; design of reactors and scaleup
with typical examples.
TOTAL: 45 PERIODS
TEXT BOOKS
1. Bailey J.E., Ollis, D.F. Biochemical Engineering Fundamentals, McGraw-Hill,
International Edition, 2nd Edition, New York, 1986.
2. Rajiv Dutta Fundamentals of Biochemical Engineering Springer I Edition 2008
REFERENCES
1. Web, F.C., Biochemical Engineering, Van Nostrand, 1964.
2. Atkinsono, B., Biochemical Reactors, Pion Ltd., 1974
1
DEPARTMENT OF CHEMICAL ENGINEERING
TWO MARKS
UNIT I INTRODUCTION TO BIOCHEMICAL ENGINEERING
1. What are the characteristic features of prokaryotic cells.

They do not contain a cell membrane bound nucleus.Procaryotes ae small and simple cells.
Prokaryotes exist in single without association with other cells. They may be spherical, rod like or spiral
and vary in size from 0.5 – 3.0μm.
2. What is the function of cell wall in prokaryotes and eukaryotes?

They are surrounded by a rigid cell wall. The thickness of the cell wall is approximately 200 A and
lends structural strength to the cell to preserve its integrity in a wide variety of external surroundings.
3. What is the function of ribosomes?

They are grainy dark spots in the interior which are of great concern to the cells involved in
biochemical reactions. These are the sites where biochemical reactions take place.
4. Give one example for different classes of prokaryotes and eukaryotes.

Prokaryotes- bacteria – Escherichia coli Eukaryotes – fungi – yeast – sacchromyces cereviseae, mold
– A.niger, algae – Euglena, protozoa – Amoeba.
5. What are endospores.

They are dormant parts of the cell which are capable of resisting heat, radiation and poisonous
chemicals. When the spores are returned to the surroundings through the cell membrane and cell wall
suitable for cell function, endospores can germinate to normal functioning cells.
2
6. Classify bacteria based on gram reaction.

Gram reaction refers to response of bacteria to a relatively straight forward and rapid staining test .
Cells are first stained with a dye crystal violet then treated with iodine solution and washed with alcohol.
In response to the gram test bacteria are classified as gram positive and gram negative .
7. Compare bacterial cell and yeast cell.

Bacterial cell Yeast cell
Show primitive cellular organization Show advanced cellular organisation
and do not possess organized nucleus and possess nucleus with a nuclear
membrane and nucleolus
Bacterial cells are motile Yeast cells are not motile
Size varies from 1-5μm Size greater than 5μm
Cytoplasm does not contain well bound Cytoplasm contains well bound organelles
organelles
Cell wall contains peptodoglycan Cell wall made up of cellulose
Cellulose is absent
8. What is mycelium.
Highly branched system of tubes which are vegetative structure of molds, higher class of fungi.
9. Compare the role of enzymes and cells in the manufacture of biochemical product.
Enzymes are proteinaceous substances present in free state within cells which activate the reaction
taking place in the cell. Cell composes of various organelles, most important of which ribosomes which
serve as active sites for enzymatic reactions.
10. What are lipids.

Lipids are biological compounds which are soluble in polar solvents such as benzene, chloroform,
ether and are practically insoluble in water. Their relative insolubility lends to their presence
predominantly in the plasma and organelle membranes.
11. What are vitamins classify them.
3
Vitamins are organic substances which are required in trace amounts for normal cell function. The
vitamins which cannot be synthesized internally by an organism are termed as essential vitamins.
Classified into 2 heads – fat soluble vitamins and water soluble vitamins.
12. What are carbohydrates.

Carbohydrates are organic compounds with general formula (CH 2O) where n >3. These compounds
are found in all animal, plant and microbial cells. They serve both structural and storage functions.
13. What is cellulose.

Cellulose is a major structural component of all plant cellsfrom algae to trees. Cellulose is the most
abundant organic compound occurring on earth. Each cellulose molecule is a long unbranched chain of
D – glucose subunits with a molecular weight ranging from 50,000 – 1,000,000.
14. What are proteins.

Proteins are most abundant organic molecules found in the cell. 30 – 70% of the cells dry weight is
protein. The prevalents components in protein are carbon, hydrogen, nitrogen and oxygen. In addition,
sulfur contributes to the three dimensional stabilization of proteins by the formation of disulfide bonds
between sulfur atoms at different locations along the polymer chain.
15. What is isoelectric point.

The acidic group ( - COOH) and basic group (-NH 2) of amino acid can ionize in aqeous solution.
The amino acid is positively charged at low pH and negatively charged at high pH. At an intermediate
pH value the amino acid acts as a dipolar ion and zwittterion which has no net charge. The pH at which
an amino acid has no net charge is termed as the isoelectric point.
16. What are actinomycetes.

Actinomycetes are a group of microorganisms with some properties of both fungi and bacteria. One
important characteristic is the susceptibity of actinomycetes to infection and disease by viruses which
can also attack bacteria.
4
17. What are the various morphological forms of bacteria.

Spirilla – rhodospirillum, cocci – streptococcus, bacilli – clostridium.
18. What are endospores. Explain their importance in bacterial cells.

Endospores are dormant parts of the cell which are capable of resisting heat, radiation and poisonous
chemicals. When the spores are returned to the surroundings throught he cell membrane and the cell
wall suitable for cell function, endospores can germinate to normal functioning cells. This normal
biologically active cell state is often called vegetative form in order to distinguigh it from the spores.
19. Give examples of bacteria capable of forming spores.

Bacillus , clostridium.
20. What are proteins.

Proteins (also known as polypeptides) are organic compoundsmade of amino acids arranged in a
linear chain and folded into a globular form. The amino acids in a polymer are joined together by
the peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
5
UNIT II ENZYMES AND ENZYME KINETICS
1. Give the nomenclature of enzymes.

Enzymes are named initially based on the substrate upon which they act.
2. What are proteolytic enzymes.

Enzymes which have the tendency of attacking nitrogen carrying compounds. Wide application in
dry cleaning as detergents.
3. Mention one parameter that differentiates catalyst from a biocatalyst.

Biocatalyst is highly specific in comparison with catalyst.
4. Give an example of an enzyme used in confectionaries.

Sacchromyces cereviseae.
5. What is the function of oxidoreductases.

Enzymes which bring about oxidation – reduction reactions, act on organic linkages to enhance
oxidation - reduction reactions.
6. What is the function of tranferases.

Enzymes which help in the transfer of functional groups are termed as transferases.
7. What is the function of hydrolases.

Hydrolases are enzymes which catalyse hydrolysis reactions.
8. How are enzymes classified.

Based on their applications.
Industrial enzymes – Analytical enzymes – medicinal enzymes.
9. Mention few commercial application of enzymes.

Amylase – glucose production – desizing textiles.
6
Pepsin – digestive aid, meat tenderizer.
10. Give the differences between chemical and biochemical reaction.
A chemical reaction is a process that leads to the transformation of one set of chemical
substances to another. Chemical reactions can be either spontaneous, requiring no input of energy, or non-
spontaneous, often coming about only after the input of some type of energy, viz. heat, light or electricity.
Classically, chemical reactions encompass changes that strictly involve the motion of electrons in the
forming and breaking of chemical bonds, although the general concept of a chemical reaction, in particular
the notion of a chemical equation, is applicable to transformations of elementary particles, as well as nuclear
reactions.
In living cells, chemical reactions that help sustain life and allow cells to grow. all chemical
processes that are produced or mediated by organisms (dominantly microbes, though all soil organisms are
probably involved). Inasmuch as most if not all soil chemical processes are either biologically produced or
biologically mediated by soil organisms, they may be considered biochemical processes. Biochemical
processes constitute one of the core elements that make up the suite of soil agents and processes termed
biodynamic agents and processes.
11. What are the major advantages of biological processes?
Advantages include:
 The design of diagnostic kits
 The creation of genome analysis tools through bioinformatics
 Genetic engineering techniques to improve food crops
 Molecular biology method to help understand the nature of diseases
 Finding targets for drugs
 Molecular breeding methods to help improve livestock
 Creation of genetically modified foods to feed the ever growing world population
 Use of DNA fingerprinting in the court of law
 Use of the PCR reaction to clone DNA and make millions of identical copies
7
 Use of stem cells to treat diseases

 Diagnosing genetic disorders
12. What are the disadvantages of biological processes?

The disadvantages include ethical and moral issues surrounding cloning and the effect this has on
society.
13. Define specificity of the enzyme.

The enzyme catalyses only one specific reaction .
14. What do you understand by sterilization.

An important aspect to be taken care of in bioprocesses unlike chemical reactions, because presence
of environmental bacteria and microorganisms consume the nutrients from the media, making the
process more difficult with the cultivation of plant or animal cells because their growth rates are much
slower than those of environmental bacteria or molds.
15. Discuss the applications of animal and vegetable proteases.
Enzymes like proteases, lipases and amylases have an important role in the soaking, dehairing,

degreasing, and bating operations of leather manufacturing.
Proteases are the most commonly used enzymes in leather production. The enzyme used
should not damage or dissolve collagen or keratin, but should be able to
hydrolyze casein, elastin, albumin and globulin-like proteins, as well as non-structured proteins which
are not essential for leather making. This process is called bating.
16. What are starch saccharifying enzymes and mention their application.
β-Amylase Malted Only a-1,4-links are cleaved, from non-reducing ends, to give limit
barley dextrins and β-maltose
Saccharifying a- B. Subtilis Only a-1,4-oligosaccharide links are cleaved to give a-dextrins with
amylase maltose, G3, G4 and up to 50% (w/w) glucose
8
17. Discuss the source and application of glucose isomerase.

D-Glucose/xylose isomerase (D-xylose ketol isomerase; ), commonly referred to as glucose
isomerase (GI), isone of the three highest tonnage value enzymes, amylase and protease being the other
two. According to Wiseman, GI may be the most important of all industrial enzymes of the future .It
catalyzes the reversible isomerization of D-glucose and D-xylose to D-fructose and D-xylulose,
respectively .Interconversion of xylose to xylulose serves a nutritional requirement in saprophytic
bacteria that thrive on decaying plantmaterial and also aids in the bioconversion of hemicellulose to
ethanol. Isomerization of glucose to fructose is of commercial importance in the production of high-
fructose corn syrup (HFCS).
18. What is the unit of enzyme activity.

Unis of enzyme activity designate the amount of enzyme which gives a certain a,certain amount of
catalytic activity under a prescribed set of standard conditions for that particular enzyme.
19. State the assumptions to derive enzyme kinetics.

Total enzyme concentration remains constant. Amount of substrate is very large in comparison with
the enzyme added. Hence depletion of substrate during enzyme substrate complex formation is assumed
negligible.
20. Mention the methods used in evaluating Michealis – Menten parameters.

Line weaver Burk plot
Langmuir plot method
Eadie – Hofstee plot method.
21. State the assumptions made in Brigg’s – Haldane approach for enzyme kinetics.
The enzymatic reaction is assumed to take place at pseudo – steady state wherein change of
intermediate substrate composition with time is negliglble.
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22. Mention the important kinetic measurements to be made over the samples removed from isothermal
vessel at different time intervals of the process.
Dry weight of microorganisms containing the enzyme, pH value, product concentration,
microscopical examination for identifying contamination.
23. Mention the various approaches used in deriving the reaction rate for any enzyme catalysed reaction
Michealis – menten approach, Brigg’s – Haldane approach.
UNIT III MICROBIAL KINETICS
1. What are the phases involved in the growth cycle of a batch cultivation.
On suspending a microbial strain into a medium containing nutrients 4 phases are involved as a part
of microbial strain growth. Lag phase, growth phase, stationary phase, death phase.
2. What are the various modes of expressing cell concentration.

Number of cells per unit volume of inoculum
Wet cell weight per unit weight of inoculum
Dry cell weight per unit weight of inoculum.
3. Is the growth rate based on cell mass and cell number identical.
The growth rate based on the number of cells and that based on cell weight are not the same. When
the mass of an individual cell increases without division, growth weight basd on cell weight increases,
while growth rate based on number of cells remains the same.
4. What is doubling time .

The time required to double cell population in any inoculum .
5. Define division rate.

Rate of cell division per unit time.
10
6. What factors control the length of lag phase in the growth cycle.
Type and age of the microorganism, size of the inoculum, culture conditions.
7. What is growth rate and what is meant by limiting nutrient.

Growth rate is defined as rate of change of cell number or cell mass w.r.to time. A nutrient whose
concentration change controls the growth rate of microorganism is termed as limiting nutrient.
8. What marks the beginning of death phase.

The toxic product buildup as a result of cell metabolisation with complete nutrient depletion .
9. What are the factors affecting cell growth.

Nutrient and toxin concentration.
10. What is the unit of specific growth rate.

1 / time.
11. What are the assumptions made in deriving growth kinetics.What are the quantitative methods for
measuring cell growth.
Cells can be represented by a single component such as cell mass, cell number, conc of protein,
DNA, RNA. The population of cell mass is distributed uniformly throughout the culture .
12. What are the mechanisms of transport across the cell.

Passive and facilitated diffusion, active transport.
13. What are the methods available for cell immobilization.

Attachment to microcarriers, entrapment within a porous matrix, containment behind a barrier.
14. What is immobilization.

Refers to confinement or localization of enzymes so that it can be reused continuously.
15. What are the functions of a semipermeable membrane.
11
Selectively permeates the essential nutrients required for cell metabolisation. Also helps in the
diffusion of fermentation products from within the cell to the inoculum.
16. What is a coenzyme.

An organic molecule of high complexity which is capable of converting an inactive protein to give a
catalytically active complex.
17. What is a cofactor.

It is a non – protein compound which combines withan inactive protein to give a catalytically active
complex.
18. Define turnover number.

The net number of substrate molecules reacting per catalyst site per unit time is turnover number.
19. What is enzyme inhibition.

The presence of a modulator would activate the enzyme activity is termed as enzyme inhibition.
20. What are the different types of inhibition.

Enzyme, substrate, product.
21. What are the factors affecting enzyme action.

Presence of modulators, pH, temperature, mechanical forces, chemical agents, irradiation.
22. What is the optimum pH for enzymatic reactions.

All enzymes do not have optimum pH value. The optimum pH of some enzymes lies in the acidic
range, some basic range. Catalytic activity of enzyme increases with increase in pH of the enzyme in
solution and passes through a maximum at the optimum pH. The catalytic activity declines smoothly
and symmetrically as pH is varied away from the optimum value.
12
23. What is substrate inhibition.

When a large amount of substrate is present, the enzyme catalysed reaction diminishes by excess
substrate concentration. This phenomenon is called substrate inhibition. When S is larger than Max S a
decrease in substrate concentration causes an increase in reaction rate.
24. Explain apoenzyme, holoenzyme and coenzyme.

A cofactor is a non protein compound which combines with an inactive protein called apoenzyme to
give a ctalytically active complex called holoenzyme. A complex organic molecule called as coenzyme
may serve as a cofactor.
25. What are modulators.

Chemical species other than substrate which combine with enzyme to alter their catalytic activity
are called modulators.
26. What are the methods available for enzyme immobilization.

Chemical – covalent bond attachment of enzymes , cross linking
Physical – entrapment of enzymes, microencapsulation of enzymes.
27. Mention the important characteristics that a support should possess.

Supports should be highly susceptible to mechanical attrition, supports should be porous.
28. What are the advantages of immobilization?

With enzymes in solution, there are chances of enzymes to leave the reactor along with the product.
This will not only need the introduction of fresh enzymes to maintain uniform concentration of enzymes
until the completion of the reaction but will also contaminate the product. Immobilisation increases the
catalytic activity efficiency of the enzymes by allowing the enzymes to remain inside the reactor till the
completion of reaction.
13
29. What is salinization?

A method for modification of support surface by coating the support with organic functional groups
by using organofunctional silane reagent. This modification enhances better attachment of the enzyme
onto the support.
30. What is microencapsulation?

An artificial method of enzyme immobilization within porous semipermeable polymeric membrane.
31. Mention some materials used in constructing microcarriers.

Ion exchange resins, dextran based beadscoated with gelatin, plyacrlamide beads, polystyrene beads,
cellulose beads.
32. Mention the disadvantages exhibited by entrapment of cells formed insitu.

Cell leakage due to cell division occurring within individual beads thereby preventing the enzymes
to remain inside the reactor to enhance further enzymatic reactions.
33. What do you understand by cross linking of enzymes.? Most widely used multifunctional
reagent is glutaraldehyde which establishes intermolecular cross links of amino groups.
UNIT IV TRANSPORT IN MICROBIAL SYSTEMS
1. Give the transport resistance in gas – liquid mass transfer.

Diffusion from bulk gas to gas – liquid interface
Movement through gas – liquid interface
Diffusion of solute through the relatively unmixed region adjacent to the bubble into the well mixed
bulk liquid
Transport of solute through the bulk liquid to a second relatively unmixed region surrounding the cells.
Transport through second unmixed liquid region associated with the cells.
Diffusive transport through cellular flock,, mycelia or soil particle.
Transport across cell envelope and into intracellular reaction site.
14
2. What are the factors affecting transport resistances in gas – liquid mass transfer.
Air bubble hydrodynamics, temperature, cellular activity, density of fermentation broth,
fermentation broth composition, interfacial area.
3. Give the names of some gas – liquid contacting molecules.

Freely rising air bubbles in contact with falling fluid as in sparged liquid fermenter.
Mechanical agitation as in stirred tank bioreactor operated in continuous or batch mode.
4. What is a sparger ?
Device used for introducing a stream of gas in the form of bubbles into a liquid.
5. What is volumetric mass transfer coefficient.

In case of packed tower fermenters interfacial area between gas and fermentation broth is not
directly measured wherein the flux of mass transfer cannot be determined but only the rate of mass
transfer as the product of flux and interfacial area may be determined. Volumetric mass transfer is
obtained by dividing the rate of mass transfer by the volume of the packing.
6. What are the factors affecting KLa values.

Liquid phase solute diffusivity, continuous phase viscosity, gas liquid interfacial resistance.
7. Define Newtonian fluid.
The ratio of shear stress and viscosity gradient.
8. Define Non – Newtonian fluid.

Fluids for which rate of shear stress is not proportional to shear strain.
Bingham plastic, pseudo plastic and fermentation broth.
9. Define sterilization.
The method of destroying foreign organisms in fermentation medium or fermentation equipment is
called sterilization.
10. What is moist heat advantages than dry heat in sterilization.
15
The intrinsic heat resistance of vegetative bacterial cells is greatly increased in completely dry state.
Death rate is much lower for dry cells than for moist cells.
Heat conduction in dry air is less rapid than in steam.
11. What is disinfection?

Disinfection is a method of sterilization to remove or reduce the risk from pathogenic organisms
using chemicals like quarternary ammonium compounds, acids and alkalies.
12. Define Del factor.

It is defined as the logarithmn of ratio of cell concentrationin terms of cell number before
sterilization and after sterilization.
13. Give the relation illustration the dependence of death rate constant on temperature.
Dependence of death rate constant on temperature is given by Arrhenius equation.
UNIT V
BIO REACTORS
1. What are microbial biosensors.

They are composed of immobilized microorganisms and an electrochemical device. These sensors
are suitable for online control of biochemical processes.
2. Name some electrodes used in construction of biosensors.

Oxygen, carbon dioxide, ammonia, pH electrodes.
3. How does contamination affect biosensors.

Contamination will affect selectivity and sensitivity of microbial sensors.
4. What are the various methods of immobilizing enzymes in microbial biosensors.

Membrane entrapment, gel entrapment.
16
5. What are the steps involved in the construction of microbial biosensors.

Culture of microorganisms, preparation of microbe immobilized membrane, construction of
microbial biosensor.
6. What is PTFE.
Poly tetra fluoro ethylene membrane used in gas sensors.
7. Give the classification of microbial biosensor.

Classified either as respiration activity measurement or electrochemically active metabolite
measurement.
8. What are the important points while immobilising microorganisms for biosensors.
In the case of oxygen electrode based sensors gas permeabilitythrough the microorganism
immobilized enzyme is important.
If it is based on the function of living cells a very gentle method for microbe immobilization must be
selected.
9. What is a thermistor.
A device used in the measurement of metabolite heat evolved from the immobilized microorganism
used in microbial biosensors.
10. Mention the steps involved in isolation of products from bioreactor broth.
Removal of particulates, primary isolation, purification.
11. What is ultrafiltration.

A membrane separation process used in the retention of molecules of size 10 to 1000 in diameter.
Useful in both product concentration and purification.
12. What is salting – out.

A purification technique used to precipitate proteins in solution using salts.
13. What is the role of spacer arm in affinity chromatographic media.
17
Provides flexibility of ligand within the matrix. Thus proteins are easily isolated.
14. Mention the advantages of using ammonium sulphate.

Highly soluble at low temperatures, less inexpensive.
15. Mention some membrane separation techniques used in protein isolation.

Microfiltration, ultrafiltration, reverse osmosis, electrophoresis.
16. What is electrophoresis.

Separation of charged species based on their specific migration rates in an electric field .
17. What factors control the separation of one protein from another in gel filtration chromatography.
Chromatography column length, rate of diffusion of protein molecules from the feed.
18. Enumerate the purpose of aeration and agitation in activated sludge reactors.
To provide oxygen for microbial respiration
To suspend and mix the sludge and other particulates
To strip out volatile metabolic products such as carbon dioxide.
19. Define bod

Defined as the amount of oxygen required for conversion of soluble convertible carbonaceous
material into insoluble material.
20. What is a fed batch reactor.

Batch reactors to which desirable liquid stream is added as the reaction process occurs unlike the
batch reactors in which feed and all required material for fermentation to take place are fed at once.
21. Give the advantage of airlift in comparison with other bioreactors.

No moving parts, simple in construction, high gas absorbance efficiency, good heat transfer.
22. Define aspect ratio.
18
The height to diameter ratio of a cylindrical bioreactor.
23. What is minimum fluidization velocity.

The superficial liquid velocity needed to just suspend the solids from a settled state .
24. State the advantages of membrane reactor.

A considerable advantage of membrane reactor lies in the fact that the biocatalyst can be used in
their native form, thus avoiding exposure to the usual inactivating steps.
25. Discuss on trickle bed reactors.
TBR are 3 phase systems containing a packed bed of heterogeneous biocatalyst and flowing gas and
liquid phases. Feed consists of both liquid and gas phase. Biochemical reaction takes place by contact
of reactant in the liquid phase and the reactant from the gas phase at the catalyst surface.
19

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CH2403 BIOCHEMICAL ENGINEERING

CH2403 BIOCHEMICAL ENGINEERING LTPC

UNIT I INTRODUCTION TO BIOCHEMICAL ENGINEERING 9

UNIT II ENZYMES AND ENZYME KINETICS 9

UNIT III MICROBIAL KINETICS 9

UNIT IV TRANSPORT IN MICROBIAL SYSTEMS 9

DEPARTMENT OF CHEMICAL ENGINEERING

UNIT I INTRODUCTION TO BIOCHEMICAL ENGINEERING

1. What are the characteristic features of prokaryotic cells.

2. What is the function of cell wall in prokaryotes and eukaryotes?

3. What is the function of ribosomes?

4. Give one example for different classes of prokaryotes and eukaryotes.

5. What are endospores.

6. Classify bacteria based on gram reaction.

7. Compare bacterial cell and yeast cell.

10. What are lipids.

11. What are vitamins classify them.

12. What are carbohydrates.

13. What is cellulose.

14. What are proteins.

15. What is isoelectric point.

16. What are actinomycetes.

17. What are the various morphological forms of bacteria.

18. What are endospores. Explain their importance in bacterial cells.

19. Give examples of bacteria capable of forming spores.

20. What are proteins.

UNIT II ENZYMES AND ENZYME KINETICS

1. Give the nomenclature of enzymes.

2. What are proteolytic enzymes.

3. Mention one parameter that differentiates catalyst from a biocatalyst.

4. Give an example of an enzyme used in confectionaries.

5. What is the function of oxidoreductases.

6. What is the function of tranferases.

7. What is the function of hydrolases.

8. How are enzymes classified.

9. Mention few commercial application of enzymes.

Pepsin – digestive aid, meat tenderizer.

10. Give the differences between chemical and biochemical reaction.

11. What are the major advantages of biological processes?

 Use of stem cells to treat diseases

12. What are the disadvantages of biological processes?

13. Define specificity of the enzyme.

14. What do you understand by sterilization.

15. Discuss the applications of animal and vegetable proteases.

Enzymes like proteases, lipases and amylases have an important role in the soaking, dehairing,

17. Discuss the source and application of glucose isomerase.

18. What is the unit of enzyme activity.

19. State the assumptions to derive enzyme kinetics.

20. Mention the methods used in evaluating Michealis – Menten parameters.

UNIT III MICROBIAL KINETICS

2. What are the various modes of expressing cell concentration.

4. What is doubling time .

5. Define division rate.

7. What is growth rate and what is meant by limiting nutrient.

8. What marks the beginning of death phase.

9. What are the factors affecting cell growth.

10. What is the unit of specific growth rate.

12. What are the mechanisms of transport across the cell.

13. What are the methods available for cell immobilization.

14. What is immobilization.

15. What are the functions of a semipermeable membrane.

16. What is a coenzyme.