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INDIABIX > Biochemical Engineering > Flashcards

Biochemical Engineering Flashcards

1
Q

A competitive inhibitor of an enzyme is usually

A

structurally similar to the substrate.

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2
Q

Linear inhibition is sometimes called as

A

complete inhibition

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3
Q

The types of inhibition pattern based on Michaelis Menten equation are
a. competitive
b. non-competitive
c. uncompetitive
d. all of the above

A

d. all of the above

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4
Q

The effect of non-competitive inhibition on a Lineweaver-Burk Plot is that

A

it can change the y-intercept

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5
Q

The rate-determining step of Michaelis Menten kinetics is

A

the complex dissociation step to produce product

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6
Q

In competitive inhibition a factor is obtained from the measurement of

A

KM

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7
Q

Which of these proteases is not a cysteine active site protease?
a. Calpain
b. Cathepsin D
c. Papain
d. None of the above

A

b. Cathepsin D

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8
Q

Given an enzyme with a Km = 10m M and Vmax = 100 m mol/min. If [S] = 100 m M, which of the following will be true?

A

A 10-fold increase in Vmax would increase velocity 10-fold y

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9
Q

The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by

A

induced fit

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10
Q

The active site of an enzyme remains
a. at the center of globular proteins
b. rigid and does not change shape
c. complementary to the rest of the molecule
d. none of the above

A

d. none of the above

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11
Q

Which category of enzymes belongs to class two in the international classification?
a. Hydrolases
b. Ligases
c. Transferases
d. Isomerase

A

Transferases

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12
Q

The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is

A

significant

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13
Q

The relationship between Keq, Km and Vmax is known as

A

Haldane equation

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14
Q

The reciprocal equation for non-competitive inhibition can be arranged to the equation for the

A

Dixon plot

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15
Q

Which of the following statements is true for enzymatically catalyzed reaction?

A

The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it

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16
Q

Which of the following common drugs is not a specific enzyme inhibitor?

A

Iodine

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17
Q

In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?

A

It changes the x-intercept

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18
Q

Which of the following statements is not true? a. Enzymes are proteins that bind to specific substrates and increase the velocity of reactions involving those substrates
b. Enzymes function by overcoming the activation energy barrier of a reaction
c. Enzymes make thermodynamically favorable reactions to proceed; they cannot make unfavorable reactions to occur
d. Enzymes only function when they are in intact cells

A

d. Enzymes only function when they are in intact cells

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19
Q

An enzyme and a reactant molecule maintain relationship as

A

a temporary association

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20
Q

An enzyme is assayed at an initial substrate concentration of 2 x 10-5M. In 6-minute, half of the substrate is used. The Km for the substrate is 2 x 10-3M. The value of k in minute is

A

0.115

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21
Q

The plot commonly used for determining the value of Vmax is
a. Lineweaver Burk plot
b. Langmuir plot
c. Eadie Hofstee plot
d. all of these

A

d. all of these

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22
Q

Quasi steady state is also known as

A

Pseudo steady state

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23
Q

Which of these enzymes contains a Zinc (Zn) ion?
a. Carboxypeptidase A
b. Phosphorylase B kinase
c. Tyrosine hydroxylase
d. Phosphodiesterase

A

Carboxypeptidase A

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24
Q

A noncompetitive inhibitor of an enzymecatalyzed reaction

A

increases KM and reduces Vmax

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25
Q

An allosteric inhibitor of an enzyme usually

A

participates in feedback regulation

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26
Q

A classical uncompetitive inhibitor is a compound that binds

A

reversibly to the enzyme substrate complex yielding an inactive ESI complex

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27
Q

Which graphical method is used to determine an enzyme degree of cooperativity?

A

Hill plot

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28
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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29
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

30
Q

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

A

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

31
Q

Classical noncompetitive inhibition is obtained only under

A

rapid equilibrium conditions

32
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

33
Q

For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be

A

0.66

34
Q

Predominantly uncompetitive inhibition may be called when

A

competitive inhibition is greater than uncompetitive inhibition

35
Q

An enzyme has a Km of 4.7 x 10-5M. If the Vmax of the preparation is 22m moles liter-1 min-1, what velocity would be observed in the presence of 2.0 x 10-4M substrate and 5.0 x 105M of a competitive inhibitor?

A

13.54μ moles liter-1min-1

36
Q

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

A

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

37
Q

Which of the following statement(s) regarding enzymes, is/are false?
a. Enzymes are always proteins that function as catalysts
b. Enzymes provide activation energy for reactions c. Enzyme activity can be regulated
d. Enzymes may be used many times for a specific reaction

A

b. Enzymes provide activation energy for reactions

38
Q

The slope of Lineweaver Burk plot for Michaelis Menten equation is

A

Km/Vmax

39
Q

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

A

1/[S] → 0

40
Q

The usual method(s) to solve rate equation of simple enzyme kinetics is/are
a. Michaelis Menten approach
b. Briggs-Haldane approach
c. Numerical solution approach
d. all of these

A

d. all of these

41
Q

Michaelis Menten equation can also be written as
a. (-Cs)/r = (Cs/rmax)+(Km/rmax)
b. 1/r = (1/rmax)+(Km/(rmax.Cs))
c. r = rmax-(Km.r/Cs)
d. All of these

A

d. All of these

42
Q

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

A

The product releasing step

43
Q

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

A

0.5 * Vmax

44
Q

A classical noncompetitive inhibitor has

A

no effect on substrate binding and vice versa

45
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

46
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

47
Q

Enzymes are basically

A

Proteins

48
Q

Which of the following refers to pseudo steady state?

A

d(CES)/dt = 0

49
Q

Which of the following refers to pseudo steady state?

A

d(CES)/dt = 0

50
Q

Most enzymes work by

A

decreasing energy of activation

51
Q

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

A

Isomerases

52
Q

Lock and key theory is based on the compatibility of

A

enzyme and substrate

53
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

54
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

55
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

56
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)

57
Q

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

A

0.1 * Vmax

58
Q

Juice clarification extraction is facilitated by using

A

Cellulases

59
Q

Lysozyme is naturally present in
a. egg white
b. bacteria
c. tears & milk
d. all of these

A

d. all of these

60
Q

Enzymes act as antimicrobials
a. by depriving an organism of a necessary metabolite
b. by generating a substances toxic to the organism
c. by attracting a cell wall component
d. all of the above

A

d. all of the above

61
Q

Trichoderma β-glucanase is reported

A

to stabilize mashing

62
Q

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

A

Protease

63
Q

Sulphydryl oxidase is used for

A

UHT milk off flavor removal

64
Q

α-amylase is an endo enzyme which requires

A

Ca

65
Q

Liquefaction of starch to dextrin is carried out by

A

α-amylase

66
Q

Milk digestibility is improved by using

A

Lactase

67
Q

Which of the following mainly serve to convert starch into high fructose corn syrup (HFCS)?
a. α-amylase
b. Gluco-isomerase
c. Gluco-amylase
d. all of these

A

d. all of these

68
Q

Lysozyme

A

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

69
Q

Hersperidinase is used for

A

juice clarification

70
Q

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

A

Cu

71
Q

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

A

Glucose oxidase-catalase

INDIABIX (8 decks)

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