2nd

Question 1

The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as

Answer 1

specific activity

Question 2

If a reaction occurs in the absence of inhibitor with rate ν0 and in the presence of inhibitor with rate νi, the degree of inhibition is defined
as

Answer 2

(ν0 - νi)/ν0

Question 3

The rate equation in competitive inhibition based on Michaelis Menten equation is given by

Answer 3

rmaxS/(Km(1+I/Ki) +S))

Question 4

Classical noncompetitive inhibition is obtained
only under

Answer 4

rapid equilibrium conditions

Question 5

In the steady state the material balance equation for any component of a system is

Answer 5

rate of addition - rate of removal + rate of
formation = 0

Question 6

Predominantly uncompetitive inhibition may be called when

Answer 6

competitive inhibition is greater than
uncompetitive inhibition

Question 7

The rate equation in non-competitive inhibition
based on Michaelis Menten equation is given
by

Answer 7

rmaxS/ (Km + S) (1+I/Ki)

Question 8

Which of the following statement(s) regarding
enzymes, is/are false?

Answer 8

Enzymes provide activation energy for
reactions

Question 9

The slope of Lineweaver Burk plot for
Michaelis Menten equation is

Answer 9

Km/Vmax

Question 10

The initial velocity, V0, of an enzyme catalyzed
reaction reaches Vmax as

Answer 10

1/[S] → 0

Question 11

The usual method(s) to solve rate equation of simple enzyme kinetics is/are

Answer 11

Michaelis Menten approach
Briggs-Haldane approach
Numerical solution approach

Question 12

Michaelis Menten equation can also be written
as

Answer 12

(-Cs)/r = (Cs/rmax)+(Km/rmax)

1/r = (1/rmax)+(Km/(rmax.Cs))

r = rmax-(Km.r/Cs)

Question 13

Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?

Answer 13

a. The substrate consuming step
**b. The product releasing step **
c. Formation of enzyme substrate complex

Question 14

When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about

Answer 14

0.5 * Vmax

Question 15

A classical noncompetitive inhibitor has

Answer 15

no effect on substrate binding and vice
versa

Question 16

The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site

Answer 16

catalyzes a chemical reaction

Question 17

Enzymes are basically

Answer 17

Proteins

Question 18

Which of the following refers to pseudo steady
state?

Answer 18

d(CES)/dt = 0

Question 19

Most enzymes work by

Answer 19

decreasing energy of activation

Question 20

Which category of enzymes belongs to class 5 in the international classification?

Answer 20

Isomerases

Question 21

Lock and key theory is based on the
compatibility of

Answer 21

enzyme and substrate

Question 22

When an enzyme is functioning at Vmax, the rate of the reaction is limited by

Answer 22

the rate at which the enzyme can convert
substrate to product

Question 23

The equation for the rate of product formation for simple enzyme reaction is given by (Where
rmax, maximum reaction rate, Cs substrate concentration, Cp product concentration ES, CES enzyme-substrate concentration)

Answer 23

rp = rmax Cs/(Km+Cs)

Question 24

When [S] = 0.1 *KM, the velocity of an enzyme catalyzed reaction is about:

Answer 24

0.1 * Vmax

Question 25

β-amylase is

Answer 25

exoenzyme saccharifying enzyme

Question 26

Juice clarification extraction is facilitated by using

Answer 26

Cellulases

Question 27

Lysozyme is naturally present in

Answer 27

a. egg white b. bacteria c. tears & milk d. all of these

Question 28

Enzymes act as antimicrobials

Answer 28

- by depriving an organism of a necessary metabolite - by generating a substances toxic to the organism - by attracting a cell wall componen

Question 29

Trichoderma β-glucanase is reported

Answer 29

to stabilize mashing

Question 30

The bitter taste of the high protein mategrials is reduced by using

Answer 30

Protease

Question 31

Sulphydryl oxidase is used for

Answer 31

UHT milk off flavor removal

Question 32

α-amylase is an endo enzyme which require

Answer 32

Ca

Question 33

Liquefaction of starch to dextrin is carried out by

Answer 33

α-amylase

Question 34

Which is true about rennet?

Answer 34

- It is a mixture of protease chymosin and pepsin - it is a mixture of rennin and pepsin

Question 35

Milk digestibility is improved by using

Answer 35

Lactase

Question 36

Which of the following mainly serve to convert starch into high fructose corn syrup (HFCS)?

Answer 36

α-amylase Gluco-isomerase Gluco-amylase

Question 37

Lysozyme

Answer 37

catalyses hydrolysis of β-1-4 linkages between N-acetyl muranic acid and N-acetyl glucosamine in peptideoglycan

Question 38

Hersperidinase is used for

Answer 38

juice clarification

Question 39

Which of the following metallic ion is there in ascorbic acid oxidase?

Answer 39

Cu

Question 40

Which of the enzyme combination is commercially used for the removal of oxygen?

Answer 40

Glucose oxidase-catalase

Question 41

The enzyme used to reduce bitterness of grapes commonly contains

Answer 41

α-L-rhamonosidase β-d-glucosidase

Question 42

Citrus juice debittering can be carried out using

Answer 42

Limoninase

Question 43

Which of the following enzyme is responsible for causing vitamin B deficiency disease beriberi?

Answer 43

Thiaminase

Question 44

Soya off flavour removal may be achieved using

Answer 44

aldehyde oxidase

Question 45

The reduction in off flavour of beer is practiced through

Answer 45

diacetyl reductase

Question 46

Discoloration can be achieved by using

Answer 46

anthocyanase

Question 47

The prosthetic group present in phenolase enzyme is

Answer 47

Cu

Question 48

Enzymes degrade, alter or synthesize a food component through

Answer 48

oxidation/reduction/isomerization hydrolysis/synthesis group transfer

Question 49

The enzyme β-galactosidase is also known as

Answer 49

isomerase

Question 50

Chymosin hydrolyses the bond between

Answer 50

Phenyl alanine and methionine