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Chemical Engineering Concepts - INDIABIX > BIOCHEMICAL ENGINEERING > Flashcards

BIOCHEMICAL ENGINEERING Flashcards

1
Q

Linear inhibition is sometimes called as

A complete inhibition
B incomplete inhibtion
C partial inhibition
D mixed inhibition

A

COMPLETE INHIBITION

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1
Q

A competitive inhibitor of an enzyme is usually

A a highly reactive compound
B a metal ion such as Hg2+ or Pb2+
C structurally similar to the substrate.
D water insoluble

A

STRUCTURALLY SIMILAR TO THE SUBSTRATE

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2
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

COMPETITIVE, NON-COMPETITIVE, UNCOMPETITIVE

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3
Q

The rate-determining step of Michaelis Menten kinetics is

A the complex formation step
B the complex dissociation step to produce product
C the product formation step
D Both (a)and(c)

A

THE COMPLEX DISSOCIATION STEP TO PRODUCE PRODUCT

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4
Q

In competitive inhibition a factor is obtained from the measurement of

A Vmax
B KM
C Y-intercept in Lineweaver-Burk Plot
D None of these

A

KM

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5
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

CATHPESIN D

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6
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

B A 10 fold decrease in Km would increase velocity

C Both (a) and (b)

D A 10 fold increase in Vmax would decrease velocity 20 fold

A

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

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7
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
B transition
C fit and fine
D Pasteur

A

INDUCED FIT

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8
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

NONE OF THE ABOVE

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9
Q

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

A it can move the entire curve to the right
B it can change the y-intercept
C it can change the x-intercept
D all of these

A

it can change the y-intercept

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10
Q

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

A Hydrolases
B Ligases
C Transferases
D Isomerase

A

TRANFERASES

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11
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 non-significant
B significant
C nothing to do with the reliability
D non significant in selected cases

A

SIGNIFICANT

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12
Q

The relationship between Keq, Km and Vmax is known as

A Haldane equation
B Michaelis Menten equation
C Numerical solution approach
D Gibbs-Helmholtz equation

A

HALDANE EQUATION

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13
Q

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

A Dixon plot
B Woolf-Augusteinsson-Hofstee plot
C Eadie-Scatchard plot
D Hanes-Woolf plot

A

DIXON PLOT

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14
Q

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

A Dixon plot
B Woolf-Augusteinsson-Hofstee plot
C Eadie-Scatchard plot
D Hanes-Woolf plot

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

B Additional substrate molecules are energized to overcome the activation energy of the reaction

C The activation energy of the reaction is increased, thus decreasing the likelihood that any substrate molecules will overcome it

D The activation energy of the reaction is lowered so that a fewer substrate molecules can overcome it

A

THE ACTIVATION ENERGY OF THE REACTION IS LOWERED SO THAT A LARGER PORTION 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
B Methotrexate
C Sulfbnilamide
D Penicillin

A

IODINE

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17
Q

The enzyme inhibition can occur by\

A reversible inhibitors
B irreversible inhibitors
C Both (a) and (b)
D None of these

A

REVERSIBLE AND IRREVERSIBLE INHIBITORS

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18
Q

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

A It moves the entire curve to right
B It moves the entire curve to left
C It changes the x-intercept
D It has no effect on the slope

A

IT CHANGES THE X-INTERCEPT

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19
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

ENZYMES ONLY FUNCTION WHEN THEY ARE IN INTACT CELSS

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20
Q

Non-competitive inhibitor of an enzyme catalyzed reaction

A decreases Vmax
B binds to Michaelis complex (ES)
C both (a) and (b)
D can actually increase reaction velocity in rare cases

A

decreases Vmax

binds to Michaelis complex (ES)

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21
Q

An enzyme and a reactant molecule maintain relationship as

A a temporary association
B an association stabilized by a covalent bond
C one in which the enzyme is changed permanently
D non complementary binding

A

A TEMPORARY ASSOCIATION

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22
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
B 0.42
C 0.093
D 6.693

A

0.115

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23
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

LINEWEAVER BURK PLOT

LANGMUIR PLOT

EADIE HOFSTEE PLOT

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24
Q

Quasi steady state is also known as

A Michaelis Menten approach
B Briggs-Haldane approach
C Pseudo steady state
D all of the above

A

PSEUDO STEADY STATE

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25
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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26
Q

A noncompetitive inhibitor of an enzyme-catalyzed reaction

A increases KM and increases Vmax
B increases KM and reduces Vmax
C reduces KM and increases Vmax
D reduces KM and reduces Vmax

A

increases KM and reduces Vmax

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27
Q

An allosteric inhibitor of an enzyme usually

A participates in feedback regulation
B denatures the enzyme
C is a hydrophobic compound
D causes the enzyme to work faster

A

PARTICIPATES IN FEEDBACK REGULATION

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28
Q

Which of the following activity is possible by transferases?

A Transfer of methyl groups
B Transfer of glycosyl group
C Both (a) and (b)
D None of these

A

Transfer of methyl groups
Transfer of glycosyl group

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29
Q

A classical uncompetitive inhibitor is a compound that binds

A reversibly to the enzyme substrate complex yielding an inactive ESI complex

B irreversibly to the enzyme substrate complex yielding an inactive ESI complex

C reversibly to the enzyme substrate complex yielding an active ESI complex

D irreversibly to the enzyme substrate complex yielding an active ESI complex

A

reversibly to the enzyme substrate complex yielding an inactive ESI complex

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30
Q

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

A Hill plot
B Koshland curve
C Michaelis-Menten hyperbola
D Can not be determined

A

HILL PLOT

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31
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
B relative activity
C purity ratio
D all of these

A

SPECIFIC ACTIVITY

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32
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
B (ν0 + νi)/ν0
C (ν0νi)/ν0
D (ν0-νi)/νi

A

(ν0 - νi)/ν0

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33
Q

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

A rmaxS/(Km (1+I/Ki)+S))
B rmaxE/(Km (1+I/Ki)+S))
C rmaxI/(Km (1+I/Ki)+S))
D rmaxS/(Km (1+I/Ki))

A

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

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34
Q

Classical noncompetitive inhibition is obtained only under

A slow equilibrium conditions
B moderate equilibrium conditions
C rapid equilibrium conditions
D non-equilibrium conditions

A

RAPID EQUILLIBRIUM CONDITIONS

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35
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

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

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

D none of the above

A

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

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36
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 0.09
B 0.33
C 0.66
D 0.91

A

0.66

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37
Q

Predominantly uncompetitive inhibition may be called when

A competitive inhibition is greater than uncompetitive inhibition

B competitive inhibition is smaller than uncompetitive inhibition

C competitive inhibition is equal to uncompetitive inhibition

D none of the above

A

COMPETITIVE INHIBITION IS GREATER THAN UNCOMPETITIVE INHIBITION

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38
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 10-5M of a competitive inhibitor?

A 13.54μ moles liter-1min-1
B 6.68μ moles liter-1min-1
C 7.57μ moles liter-1min-1
D 17.8μ moles liter-1min-1

A

13.54μ moles liter-1min-1

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39
Q

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

A rmaxS/(Km + S)(1+I/Ki)
B rmaxE/(Km (1+I/Ki)+S))
C VmaxS/(Km + S)(1+I/Ki)
D rmaxS/Km

A

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

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40
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

ENZYMES PROVIDE ACTIVATION ENERGY FOR REACTIONS

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41
Q

The slope of Lineweaver Burk plot for Michaelis Menten equation is

A Vmax/Km
B Km/Vmax
C 1/Km
D Km.Vmax

A

Km/Vmax

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42
Q

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

A [S] = KM
B [S] = 10 * KM
C 1/[S] = 1/KM
D 1/[S] → 0

A

1/[S] → 0

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43
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

Michaelis Menten approach

Briggs-Haldane approach

Numerical solution approach

44
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

ALL OF THESE

45
Q

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

A The substrate consuming step
B The product releasing step
C Formation of enzyme substrate complex
D None of these

A

THE PRODUCT RELEASING STEP

46
Q

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

A 0.1 * Vmax
B 0.2 * Vmax
C 0.5 * Vmax
D 0.9 * Vmax

A

0.5 * Vmax

47
Q

A classical noncompetitive inhibitor has

A no effect on substrate binding

B no effect on substrate binding and vice versa

C significant effect on substrate binding

D significant effect on substrate binding and vice versa

A

NO EFFECT ON SUBSTRATE BUILDING AND VICE VERSA

48
Q

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

A contains modified amino acids
B catalyzes a chemical reaction
C is complementary to a specific ligand
D contains amino acids without side chains

A

CATALYZES A CHEMICAL REACTION

49
Q

Enzymes are basically

A proteins
B vitamins
C fat
D carbohydrate

A

PROTEINS

50
Q

Which of the following refers to pseudo steady state ?

A d(CE)/dt = 0
B d(Cp)/dt = 0
C d(CES)/dt = 0
D d(Cs)/dt = d(CES)/dt

A

d(CES)/dt = 0

51
Q

Most enzymes work by

A increasing energy of activation
B decreasing energy of activation
C not affecting energy of activation
D none of the above

A

DECREASING ENERGY OF ACTIVATION

52
Q

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

A Hydrolases
B Isomerases
C Oxido-reductases
D Cyclase

A

ISOMERASES

53
Q

Lock and key theory is based on the compatibility of

A enzyme and substrate
B enzyme and product
C enzyme and enzyme substrate complex
D enzyme substrate complex and product

A

ENZYME AND SUBSTRATE

54
Q

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

A the number of collisions between enzyme and substrate
B the number of substrate molecules in the reaction
C the concentration of the substrate
D the rate at which the enzyme can convert substrate to product

A

THE RATE AT WHICH THE ENZYME CAN CONVERT SUBSTRATE TO PRODUCT

55
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)
B rp= rmax CES/(Km+ CES)
C rp = rmax Cs/(Km+CES)
D rp = rmax Cs/(Km+Cp)

A

rp = rmax Cs/(Km+Cs)

56
Q

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

A 0.1 * Vmax
B 0.3 * Vmax
C 0.5 * Vmax
D 0.7 * Vmax

A

0.1 * Vmax

57
Q

β-amylase is

A endoenzyme
B exoenzyme
C saccharifying enzyme
D both (b) and (c)

A

EXOENZYME
SACCHARIFYIN ENZYME

58
Q

Juice clarification extraction is facilitated by using

A cellulases
B amylase
C inulinase
D lactase

A

CELLULASES

59
Q

Lysozyme is naturally present in

A egg white
B bacteria
C tears & milk
D all of these

A

EGG WHITE, BACTERIA, TEARS AND MILK

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

ALL A B C

61
Q

Trichoderma β-glucanase is reported

A to stabilize mashing
B to convert taste fractions of dextrins to fermentable sugars in beer
C to convert starch to dextrin
D all of the above

A

TO STABILIZE MASHING

62
Q

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

A invertase
B dectinase
C protease
D none of these

A

PROTEASE

63
Q

Sulphydryl oxidase is used for

A discoloration
B clarification of images
C UHT milk off flavour removal
D all of these

A

UHT MILK OFF FLAVOR REMOVAL

64
Q

α-amylase is an endo enzyme which requires

A Ca
B Cu
C Mn
D None of these

A

CA

65
Q

Liquefaction of starch to dextrin is carried out by

A α-amylase
B cellulase
C pectinase
D all of these

A

α-amylase

66
Q

Which is true about rennet?

A It is a mixture of protease chymosin and pepsin
B It is a mixture of rennin and pepsin
C Both (a) and (b)
D none of the above

A

It is a mixture of protease chymosin and pepsin

It is a mixture of rennin and pepsin

67
Q

Milk digestibility is improved by using

A RNase
B lactase
C β-amylase
D none of these

A

LACTASE

68
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

α-amylase

Gluco-isomerase

Gluco-amylase

69
Q

Lysozyme

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

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

C catalyses hydrolysis of α-1-4 linkages between N-diacetyl muranic acid and N-diacetyl glucosamine in peptideoglycan

D all of the above

A

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

70
Q

Hersperidinase is used for

A juice clarification
B juice debittering
C off flavour reduction
D RNA reduction in fish

A

JUICE CLARIFICATION

71
Q

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

A Mg
B Fe
C Cu
D Mn

A

CU

72
Q

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

A Glucose oxidase-cellulase
B Glucose oxidase-catalase
C Glucose oxidase-lactase
D All of these

A

GLUCOSE OXIDASE-CATALASE

73
Q

The enzyme used to reduce bitterness of grapes commonly contains

A α-L-rhamonosidase
B β-d-glucosidase
C β- galactosidase
D both (a) and (b)

A

α-L-rhamonosidase

β-d-glucosidase

74
Q

Citrus juice debittering can be carried out using

A limoninase
B inulinase
C anthocyanase
D None of these

A

LIMONINASE

75
Q

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

A Ascorbic acid oxidase
B Thiaminase
C Lipoxygenase
D None of these

A

THIAMINASE

76
Q

Soya off flavour removal may be achieved using

A di acetyl reductase
B β- amylase
C aldehyde oxidase
D protease

A

ALDEHYDE OXIDASE

77
Q

The reduction in off flavour of beer is practiced through

A hersperidinase
B rnase
C invertase
D diacetyl reductase

A

DIACETYL REDUCTASE

78
Q

Discoloration can be achieved by using

A sulphloydryl oxidase
B proteases
C anthocyanase
D all of these

A

ANTHOCYANASE

79
Q

The prosthetic group present in phenolase enzyme is

A Mg
B Cu
C Ca
D Fe

A

CU

80
Q

Enzymes degrade, alter or synthesize a food component through

A oxidation/reduction/isomerization
B hydrolysis/synthesis
C group transfer
D all of the above

A

oxidation/reduction/isomerization
hydrolysis/synthesis
group transfer

81
Q

The enzyme β-galactosidase is also known as

A lactase
B EC3.2.1.23
C both (a) and (b)
D isomerase

A

lactase
EC3.2.1.23

82
Q

Chymosin hydrolyses the bond between

A Alanine and glycine
B Phenyl alanine and methonine
C Glutamic acid and alanine
D Alanine and phenyl alanine

A

PHENYL ALANINE AND METHONINE

83
Q

The function of the disengagement zone in an airlift fermenter is to

A prevent CO2 rich bubbles from entering the downcomer
B reduce the velocity of the bubbles
C reduce liquid loss as aerosols
D all of the above

A

ALL OF THE ABOVE

84
Q

Stationary phase is described as

A no further increase in the cell population after a maximum value

B deceleration of growth and division rate after the growth rate reaches a maximum

C acceleration of growth and division rate after the growth rate reaches a maximum

D deceleration of growth and division rate after the growth rate reaches a minimum

A

NO FURTHER INCREASE IN THE CELL POPULATION AFTER MAXIMUM VALUE

85
Q

In the accelerated phase, cell starts to

A increase and the division rate increases to reach a maximum

B decrease and the division rate increases to reach a maximum

C increase and the division rate decreases to reach a maximum

D increase and the division rate increases to reach a minimum

A

increase and the division rate increases to reach a maximum

86
Q

The monod model predicts that the specific growth rate

A will increase with the concentration of the growth limiting substrate until it reaches a
maximum value

B will decrease with the concentration of the growth limiting substrate

C will increase with the concentration of the growth limiting substrate

D does not depend on growth limiting substrate

A

WILL INCREASE WITH THE CONCENTRATION OF THE GROWTH LIMITING SUBSTRATE UNTIL IT REACHES A MAXIMUM VALUE

87
Q

A mixed fermentation is one, which produces

A both alcohol and carbon dioxide
B both acid and carbon dioxide
C both acid and alcohol
D several different kinds of acid

A

BOTH ACID AND ALCOHOL

88
Q

The function of a mechanical seal is to

A prevent contaminants entering the reactor
B prevent cells from leaving the reactor
C both (a) and (b)
D prevent air to enter

A

PREVENT CONTAMINANTS ENTERING THE REACTOR

PREVENT CELLS FROM LEAVING THE REACTOR

89
Q

The phenomenon in which substrates are used in a sequential manner is known as

A trans-substrate genesis
B dialism
C diauxie
D multiplicity

A

DIAUXIE

90
Q

The dilution rate, D is defined as(where F = volumetric flow rate, VR = total volume of culture in the reactor and μ specific growth rate)

A F/VR
B VR/F
C μ/F
D F/μ

A

F/VR

91
Q

Diauxie is

A growth factors
B microbiological die off
C the simultaneous uptake of nutrients
D the stagewise uptake of nutrients

A

THE STAGEWISE UPTAKE OF NUTRIENTS

92
Q

An open system in which the growth rate is maintained by adding a nutrient (present in limiting quantities) at the same rate as that medium containing micro-organisms is removed is called

A manostat
B chemostat
C turbidostat
D culturostat

A

CHEMOSTAT

93
Q

In the death phase

A nutrients available for the cells are depleted and begin to die
B the number of viable cells will increase
C nutrients available for cells are replenished and start to multiply
D none of the above

A

NUTRIENTS AVAILABLE FOR THE CELLS ARE DEPLERED AND BEGIN TO DIE

94
Q

The maximum specific growth rate of an organism depends on

A medium composition
B temperature
C pH
D All of these

A

MEDIUM COMPOSITION, TEMPERATURE, PH

95
Q

Which of the following is not correct for the Monod model and the Michaelis Menten Model?

A The Michaelis Menten Model was derived from a curve fitting exercise

B The Michaelis Menten model was derived from an analysis of the
mechanism of microbial growth

C The Monod model was derived from an analysis of the mechanism of microbial growth

D All of the above

A

THE MONOD MODEL WAS DERIVED FROM AN ANALYSIS OF THE MECHANISM OF MICROBIAL GROWTH

96
Q

Bubble column reactor has

A large height to diameter ratio
B small height to diameter ratio
C large diameter to height ratio
D small diameter to height ratio

A

LARGE HEIGTH TO DIAMETER RATIO

97
Q

Why a T-flask used in small-scale cell culture is incubated in a horizontal position?

A To save space
B To increase the surface area of the liquid-air interface
C Both (a) and (b)
D To increase the rate of oxygen transfer into the liquid

A

To save space

To increase the surface area of the liquid-air interface

98
Q

An open system in which the growth rate is maintained by the removal and addition of media at such a rate as to maintain a constant cell density is called a

A manostat
B chemostat
C turbidostat
D culturostat

A

TURBIDOSTAT

99
Q

Wash out in steady state fermentation occurs when

A dilution rate is less than maximum specific growth rate

B dilution rate is higher than the maximum specific growth rate

C cell concentration reaches the maximum

D specific growth rate is maximum

A

DILUTION RATE IS HIGHER THAN THE MAXIMUM SPECIFIC GROWTH RATE

100
Q

Fermentor should be filled with medium upto

A 65-70%
B 70-75%
C 75-80%
D 80-85%

A

75% TO 80%

101
Q

Bacterial growth curve is obtained by plotting

A number of cells versus time
B number fo spores versus time
C log of number of cells versus time
D log of number of cells survived versus time

A

LOG OF NUMBER OF CELLS VERSUS TIME

102
Q

When intracellular enzymes of whole cells are to be used in a bio-conversion process, it is often necessary to____________the cells.

A permeabilize
B lyophilize
C heat-kill
D denature

A

PERMEABILIZE

103
Q

Heat transfer rates (per unit volume) will be lowest in

A Stirred tank bioreactor with biomass recycle
B Continuous air lift bioreactor
C Continuous packed bed reactor
D Continuous fluidized bed bioreactor

A

CONTINUOUS PACKED BED REACTOR

104
Q

The function(s) of the draft tube in an airlift bioreactor is

A to reduce bubble coalescence
B to improve circulation
C to even out shear conditions throughout the reactor
D all of the above

A

TO REDUCE BUBBLE COALAESCENCE

TO IMPROVE CIRCULATION

TO EVEN OUT SHEAR CONDITIONS THROUGHOUT THE REACTOR

105
Q

The Monod Model relates

A substrate utilized with the biomass consumption

B specific growth rate to the substrate availability

C yield with the biomass utilization

D the biomass concentration with specific growth rate

A

SPECIFIC GROWTH RATE TO THE SUBSTRATE AVAILABILITY

106
Q

The height to diameter ratio (H/D) for the column fermenters is

A <3
B >3
C <1.5
D >1.5

A

> 3

107
Q
A

Chemical Engineering Concepts - INDIABIX (2 decks)

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