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Boredom 1: Bio Chem > 2nd > Flashcards

2nd Flashcards

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1
Q

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

A

specific activity

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2
Q

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

A

(ν0 - νi)/ν0

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3
Q

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

A

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

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4
Q

Classical noncompetitive inhibition is obtained
only under

A

rapid equilibrium conditions

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5
Q

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

A

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

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6
Q

Predominantly uncompetitive inhibition may be called when

A

competitive inhibition is greater than
uncompetitive inhibition

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7
Q

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

A

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

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8
Q

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

A

Enzymes provide activation energy for
reactions

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9
Q

The slope of Lineweaver Burk plot for
Michaelis Menten equation is

A

Km/Vmax

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10
Q

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

A

1/[S] → 0

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11
Q

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

A

Michaelis Menten approach
Briggs-Haldane approach
Numerical solution approach

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12
Q

Michaelis Menten equation can also be written
as

A

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

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

r = rmax-(Km.r/Cs)

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13
Q

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

A

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

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14
Q

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

A

0.5 * Vmax

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15
Q

A classical noncompetitive inhibitor has

A

no effect on substrate binding and vice
versa

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16
Q

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

A

catalyzes a chemical reaction

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17
Q

Enzymes are basically

A

Proteins

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18
Q

Which of the following refers to pseudo steady
state?

A

d(CES)/dt = 0

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19
Q

Most enzymes work by

A

decreasing energy of activation

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20
Q

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

A

Isomerases

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21
Q

Lock and key theory is based on the
compatibility of

A

enzyme and substrate

22
Q

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

A

the rate at which the enzyme can convert
substrate to product

23
Q

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)

A

rp = rmax Cs/(Km+Cs)

24
Q

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

A

0.1 * Vmax

25
Q

β-amylase is

A

exoenzyme
saccharifying enzyme

26
Q

Juice clarification extraction is facilitated by
using

A

Cellulases

27
Q

Lysozyme is naturally present in

A

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

28
Q

Enzymes act as antimicrobials

A
  • by depriving an organism of a necessary
    metabolite
  • by generating a substances toxic to the
    organism
  • by attracting a cell wall componen
29
Q

Trichoderma β-glucanase is reported

A

to stabilize mashing

30
Q

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

A

Protease

31
Q

Sulphydryl oxidase is used for

A

UHT milk off flavor removal

32
Q

α-amylase is an endo enzyme which require

A

Ca

33
Q

Liquefaction of starch to dextrin is carried out
by

A

α-amylase

34
Q

Which is true about rennet?

A
  • It is a mixture of protease chymosin and pepsin
  • it is a mixture of rennin and pepsin
35
Q

Milk digestibility is improved by using

A

Lactase

36
Q

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

A

α-amylase
Gluco-isomerase
Gluco-amylase

37
Q

Lysozyme

A

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

38
Q

Hersperidinase is used for

A

juice clarification

39
Q

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

A

Cu

40
Q

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

A

Glucose oxidase-catalase

41
Q

The enzyme used to reduce bitterness of grapes
commonly contains

A

α-L-rhamonosidase
β-d-glucosidase

42
Q

Citrus juice debittering can be carried out using

A

Limoninase

43
Q

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

A

Thiaminase

44
Q

Soya off flavour removal may be achieved
using

A

aldehyde oxidase

45
Q

The reduction in off flavour of beer is practiced
through

A

diacetyl reductase

46
Q

Discoloration can be achieved by using

A

anthocyanase

47
Q

The prosthetic group present in phenolase
enzyme is

A

Cu

48
Q

Enzymes degrade, alter or synthesize a food
component through

A

oxidation/reduction/isomerization
hydrolysis/synthesis
group transfer

49
Q

The enzyme β-galactosidase is also known as

A

isomerase

50
Q

Chymosin hydrolyses the bond between

A

Phenyl alanine and methionine

Boredom 1: Bio Chem (4 decks)

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