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MCQOPTIONS
This section includes 79 Mcqs, each offering curated multiple-choice questions to sharpen your Enzyme Science knowledge and support exam preparation. Choose a topic below to get started.
| 1. |
E. coli cell culture (1 ml) was diluted 1:1000000 and 200 l of this was used for plating. After 12h incubation of the plate, the number of colony forming units (CFU) was 150. What is the total CFUper ml in original culture ? |
| A. | 7.5 10 |
| B. | 1.5 10 |
| C. | |
| D. | 1.5 10 |
| E. | 3.0 10 |
| Answer» B. 1.5 10 | |
| 2. |
Using the Hill equation for an enzyme [S]0 = (v0 Km/ Vmax v0)1/n and the plot of log10(v0/Vmax v0) vs log 10 [S]0 one can find out(P) Vmax form the intercept on the ordinate (Q) Km form the intercept on the ordinalte(R) n from the slope (S) Km from the intercept on the abscissa |
| A. | P, Q |
| B. | Q, R |
| C. | R, S |
| D. | P, S |
| Answer» E. | |
| 3. |
Match the following products with their starting substrates A. Sake 1. apple juiceB. cider2. grape juiceC. wine3. barleyD. lager4. rice/td> |
| A. | A 4, B 1, C 2, D 3 |
| B. | A 1, B 4, C 2, D 3 |
| C. | A 2, B 3, C 1, D 4 |
| D. | A 3, B 4, C 2, D 1 |
| Answer» B. A 1, B 4, C 2, D 3 | |
| 4. |
An enzyme following Michaelis Menten kinetics with Vm = 2.5 mmol m 3 s 1 and Km = 5.0 mM was used to carry out the reaction in a batch stirred reactor. Starting with an initial substrate concentration of 0.1 M. The time required for 50% conversion of the substrate will be about |
| A. | 01 hr |
| B. | 06 hr |
| C. | 02 hr |
| D. | 12 hr |
| Answer» C. 02 hr | |
| 5. |
The two columns given below indicate some of the fermentation products and the microbial cultures used for their production. Identify the correct set of groups from the four options. Fermentation Microbial productscultures (A) Ethanol (P) Aspergillus niger (B) Streptomycin (Q) Zymomonas mobiles (C) Citric acid (R) Streptomyces griseus(D) Cellulase (S) Trichoderma reesei |
| A. | A-P; B-Q; C-R; D-S |
| B. | A-Q; B-R; C-P; D-S |
| C. | A-Q; B-R; C-S; D-P |
| D. | A-S; B-R; C-Q; D-P |
| Answer» C. A-Q; B-R; C-S; D-P | |
| 6. |
Immobilization of enzymes (P) increases the specificity of the enzyme for its reactants (Q) facilitates reuse of the enzyme in batch reactions (R) makes it unsuitable for its use in a continuous reactor system(S) decreases the operational cost of the industrial process |
| A. | Q, S |
| B. | Q, R |
| C. | R, S |
| D. | P, Q |
| Answer» B. Q, R | |
| 7. |
Immobilization of enzymes using entrapment method requires (P) photosensitive polyethylene glycol dimethacrylate (Q) CNBr activation of sepharose (R) polyfunctional reagent like hexamethylene diisocyanate (S) radiation of polyvinyl alcohol |
| A. | P, Q |
| B. | R, S |
| C. | P, S |
| D. | Q, S |
| Answer» D. Q, S | |
| 8. |
Km values of enzyme X for substrate S1 and S2 are 0.1 mM and 0.01 mM, respectively This suggest that P. enzyme X has more affinity towards S1 Q. enzyme X has low affinity towards S1 R. enzyme X has more affinity towards S2 S. enzyme X has low affinity towards S2 |
| A. | P, Q |
| B. | R, S |
| C. | Q, S |
| D. | Q, R |
| Answer» E. | |
| 9. |
Determine the correctness or otherwise of the following Assertion [a] and Reason [r] Assertion : Enzymatic method of tissue dispersion is milder than chemical and mechanical methods. Reason : Enzymes work at optimal temperature and pH |
| A. | Both [a] and [r] are true and [r] is the correct reason for [a] |
| B. | Both [a] and [r] are true but [r] is not the correct reason for [a] |
| C. | [a] is true but [r] is false |
| D. | [a] is false but [r] is true |
| Answer» C. [a] is true but [r] is false | |
| 10. |
Match the industrial application of the following enzymes P Penicillinase1. PharmaceuticalQ Pectinase2. LeatherR Trypsin3. WineS Rennin4. Dairy/td> |
| A. | P-4 P-l P-l P-4 |
| B. | Q-3 Q-3 Q-2 Q-2 |
| C. | R-l R-2 R-3 R-3 |
| D. | S-2 S-4 S-4 S-l |
| Answer» C. R-l R-2 R-3 R-3 | |
| 11. |
The same culture (with the m and Ks values as computed above) is cultivated in a 10-litre chemostat being operated with a 50 ml/min sterile feed containing 50 g/l of substrate. Assuming an overall yield coefficient of 0.3 g-DCW/g-substrate, the respective values of the outlet biomass and substrate concentration are |
| A. | 15 g/l, 48 mg/l |
| B. | 15 g/l, 0.48 g/l |
| C. | 48 g/l, 15 g/l |
| D. | 4.8 g/l, 4.8 g/l |
| Answer» B. 15 g/l, 0.48 g/l | |
| 12. |
Analysis of a hexapeptide using enzymatic cleavage reveals the following result: Amino acid composition of the peptide is: 2R, A,V, S, Y Trypsin digestion yields two fragments and the compositions are: (R, A, V) and (R, S, Y) Chymotrypsin digestion yields two fragments and the compositions are: (A, R, V, Y) and (R, S) Digestion with carboxypeptidase A yields no cleavage product. Given: Trypsin cleaves at carboxyl side of R. Chymotrypsin cleaves at carboxyl side of Y. Carboxypeptidase A cleaves at amino side of the C-terminal amino acid (except R and K) of the peptide. The correct amino acid sequence of the peptide is: |
| A. | RSYRVA |
| B. | AVRYSR |
| C. | SRYVAR |
| D. | SVRRYA |
| Answer» C. SRYVAR | |
| 13. |
The activity of lactate dehydrogenase can be measured by monitoring the following reaction: Pyruvate + NADH Lactate + NAD+The molar extinction coefficient of NADH at 340 nm is 6220 M 1.cm 1.NAD+ does not absorb at this wavelength. In an assay, 25 L of a sample of enzyme (containing 5 g protein per mL) was added to a mixture of pyruvate and NADH to give a total volume of 3 mL in a cuvette of 1 cm pathlength. The rate of decrease in absorbance at 340 nm was 0.14 min 1. The specific activity of the enzyme will be _________ mol.min 1.mg 1. |
| A. | 628.5 : 725.58 |
| B. | 845.5 : 958.4 |
| C. | 525.0 : 555.0 |
| D. | 225.5 : 452.8 |
| Answer» D. 225.5 : 452.8 | |
| 14. |
In an assay of the type II dehydroquinase of molecular mass 18 kDa, it is found that the Vmax of the enzyme is 0.0134 mol.min 1 when 1.8 g enzyme is added to the assay mixture. If the Km for the substrate is 25 M, the kcat/Km ratio will be _____ 104 M 1.s 1. |
| A. | 7.5 : 10.05 |
| B. | 8.5 : 8.9 |
| C. | 10.85: 14.89 |
| D. | 8.6 : 9.4 |
| Answer» E. | |
| 15. |
Identify the enzyme that catalyzes the following reaction -Ketoglutarate + NADH + NH4+ + H+ ? Glutamate + NAD+ + H2O |
| A. | Glutamate synthetase |
| B. | Glutamate oxoglutarate aminotransferase |
| C. | Glutamate dehydrogenase |
| D. | -ketoglutarate deaminase |
| Answer» D. -ketoglutarate deaminase | |
| 16. |
The turnover numbers for the enzymes, E1 and E2 are 150 s 1 and 15 s 1 respectively. This means |
| A. | E1 binds to its substrate with higher affinity than E2 |
| B. | The velocity of reactions catalyzed by E1 and E2 at their respective saturating substrate concentrations could be equal, if concentration of E2 used is 10 times that of E1 |
| C. | The velocity of E1 catalyzed reaction is always greater than that of E2 |
| D. | The velocity of E1 catalyzed reaction at a particular enzyme concentration and saturating substrate concentration is lower than that of E2 catalyzed reaction under the same conditions |
| Answer» C. The velocity of E1 catalyzed reaction is always greater than that of E2 | |
| 17. |
The respective values of the Monod kinetic constants m (hr 1) and Ks (mg/l) are as follows: |
| A. | 0.08, 8 |
| B. | 0.8, 0.8 |
| C. | 0.8, 80 |
| D. | 8, 8 |
| Answer» D. 8, 8 | |
| 18. |
After completion of Nick translation reaction, 10 l of reaction was spotted on a glass-fiber filter that upon counting resulted into 4.2 104 cpm in reaction. Another 10 l was processed for TCA precipitation to determine redioisotope incorporation. The TCA precipitated sample gave 2.94 104 cpm. What is the percent of [ -32P]-dCTP incorporation into the DNA sample? |
| A. | 40% |
| B. | 50% |
| C. | 60% |
| D. | 70% |
| Answer» E. | |
| 19. |
In a chemostat, evaluate the dilution rate at the cell wash-out condition by applying Monod smodel with the given set of data: max = 1h 1;Yx/s = 0.5 g g 1; Ks = 0.2 g L 1; S0 = 10 g L 1 |
| A. | 1.00 h |
| B. | 0.49 h |
| C. | |
| D. | 0.98 h |
| E. | 1.02 h |
| Answer» D. 0.98 h | |
| 20. |
An enzyme is immobilized on the surface of a non-porous spherical particle of 2 mm diameter. The immobilized enzyme is suspended in a solution having bulk substrate concentration of 10 mM. The enzyme follows first order kinetics with rate constant 10 s 1 and the external mass transfer coefficient is 1 cm.s 1. Assume steady state condition wherein rate of enzyme reaction (m mol.L 1.s 1) at the surface is equal to mass transfer rate (m mol.L 1.s 1). The substrate concentration at the surface of the immobilized particle will be ________ mM. |
| A. | 8.5 : 8.5 |
| B. | 7.5 : 7.5 |
| C. | 5.5 : 5.5 |
| D. | 2.5 : 2.5 |
| Answer» C. 5.5 : 5.5 | |
| 21. |
Choose the CORRECT combination of True (T) and False (F) statements about microcarriers used in animal cell culture. P. Higher cell densities can be achieved using microcarriersQ. Microcarriers increase the surface area for cell growth R. Microcarriers are used for both anchorage- and nonanchorage-dependent cells S. Absence of surface charge on microcarriers enhances attachment of cells |
| A. | P-T, Q-F, R-T and S-F |
| B. | P-T, Q-T, R-F and S-F |
| C. | P-F, Q-F, R-T and S-T |
| D. | P-F, Q-T, R-F and S-T |
| Answer» C. P-F, Q-F, R-T and S-T | |
| 22. |
The Ki of novel competitive inhibitor designed against an enzyme is 2.5 M. The enzyme was assayed in the absence or presence of the inhibitor (5 M) under identical conditions. The Km in the presence of the inhibitor was found to be 30 M. The Km in the absence of the inhibitor is ____ M. |
| A. | 80 or 30 |
| B. | 100 or 40 |
| C. | 90 or 10 |
| D. | 60 or 100 |
| Answer» D. 60 or 100 | |
| 23. |
A single subunit enzyme converts 420 moles of substrate to product in one minute. The activity of the enzyme is ______ 10 6 Katal. |
| A. | 1 |
| B. | 3 |
| C. | 5 |
| D. | 7 |
| Answer» E. | |
| 24. |
A chemostat is operating at steady state at a dilution rate of 0.1 hr 1 and a limiting nutrient concentration of 10 M. If max for the organism is 0.5 hr 1. Calculate the Monod constant for the nutrient.(b) Why asparaginase is used in anticancer therapy? |
| A. | Abzyme is a monoclonal antibody with catalytic activity. Abzymes are usually artificial constructs, but are also found in normal and in patients with autoimmune diseases such as systemic lupus erythematosus, where they can bind to and hydrolyze DNA. |
| B. | Enzyme is a monoclonal antibody with catalytic activity. Abzymes are usually artificial constructs, but are also found in normal and in patients with autoimmune diseases such as systemic lupus erythematosus, where they can bind to and hydrolyze DNA. |
| C. | Both A and B |
| D. | None of the above |
| Answer» B. Enzyme is a monoclonal antibody with catalytic activity. Abzymes are usually artificial constructs, but are also found in normal and in patients with autoimmune diseases such as systemic lupus erythematosus, where they can bind to and hydrolyze DNA. | |
| 25. |
The factor (s) likely to increase the rate of reaction catalyzed by a surface immobilized enzyme is/are |
| A. | Increased agitation of the bulk liquid containing the substrate |
| B. | Continued replacement of the bulk liquid containing the substrate |
| C. | Increased concentration of the substrate in the bulk liquid |
| D. | All of these |
| Answer» C. Increased concentration of the substrate in the bulk liquid | |
| 26. |
An immobilized enzyme being used in a continuous plug flow reactor exhibits an effectiveness factor ( ) of 1.2. The value of being greater than one could be apparently due to one of the following reasons. Identify the correct reason. |
| A. | The enzyme follows substrate inhibited kinetics with internal pore diffusion limitation |
| B. | The enzyme experiences external film diffusion limitation |
| C. | The enzyme follows sigmoidal kinetics |
| D. | The immobilized enzyme is operationally unstable |
| Answer» B. The enzyme experiences external film diffusion limitation | |
| 27. |
Immobilization of enzymes using entrapment method requires |
| A. | P, Q |
| B. | R, S |
| C. | P, S |
| D. | Q, S |
| Answer» D. Q, S | |
| 28. |
K |
| A. | P, Q |
| B. | R, S |
| C. | Q, S |
| D. | Q, R |
| Answer» E. | |
| 29. |
Determine the correctness or otherwise of the following Assertion [a] and Reason [r] |
| A. | Both [a] and [r] are true and [r] is the correct reason for [a] |
| B. | Both [a] and [r] are true but [r] is not the correct reason for [a] |
| C. | [a] is true but [r] is false |
| D. | [a] is false but [r] is true |
| Answer» C. [a] is true but [r] is false | |
| 30. |
The same culture (with the |
| A. | 15 g/l, 48 mg/l |
| B. | 15 g/l, 0.48 g/l |
| C. | 48 g/l, 15 g/l |
| D. | 4.8 g/l, 4.8 g/l |
| Answer» B. 15 g/l, 0.48 g/l | |
| 31. |
Using the Hill equation for an enzyme [S] |
| A. | P, Q |
| B. | Q, R |
| C. | R, S |
| D. | P, S |
| Answer» E. | |
| 32. |
Match the following products with their starting substrates |
| A. | A 4, B 1, C 2, D 3 |
| B. | A 1, B 4, C 2, D 3 |
| C. | A 2, B 3, C 1, D 4 |
| D. | A 3, B 4, C 2, D 1 |
| Answer» B. A 1, B 4, C 2, D 3 | |
| 33. |
The number of ligand binding sites present on receptors R1 and R3, respectively are |
| A. | 1 and 4 |
| B. | 1 and 1 |
| C. | 4 and 1 |
| D. | 2 and 2 |
| Answer» E. | |
| 34. |
Immobilization of enzymes |
| A. | Q, S |
| B. | Q, R |
| C. | R, S |
| D. | P, Q |
| Answer» B. Q, R | |
| 35. |
An enzyme following Michaelis Menten kinetics with V |
| A. | 01 hr |
| B. | 06 hr |
| C. | 02 hr |
| D. | 12 hr |
| Answer» C. 02 hr | |
| 36. |
An enzymatic reaction is described by the following rate expression. |
| A. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-20A.png"> |
| B. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-20B.png"> |
| C. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-20C.png"> |
| D. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-20D.png"> |
| Answer» B. <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-20B.png"> | |
| 37. |
The two columns given below indicate some of the fermentation products and the microbial cultures used for their production. Identify the correct set of groups from the four options. |
| A. | A-P; B-Q; C-R; D-S |
| B. | A-Q; B-R; C-P; D-S |
| C. | A-Q; B-R; C-S; D-P |
| D. | A-S; B-R; C-Q; D-P |
| Answer» C. A-Q; B-R; C-S; D-P | |
| 38. |
Which one of the receptors has thehighestaffinity for the ligand? |
| A. | R1 |
| B. | R2 |
| C. | R3 |
| D. | R4 |
| Answer» B. R2 | |
| 39. |
Analysis of a hexapeptide using enzymatic cleavage reveals the following result: |
| A. | RSYRVA |
| B. | AVRYSR |
| C. | SRYVAR |
| D. | SVRRYA |
| Answer» C. SRYVAR | |
| 40. |
The activity of lactate dehydrogenase can be measured by monitoring the following reaction: |
| A. | 628.5 : 725.58 |
| B. | 845.5 : 958.4 |
| C. | 525.0 : 555.0 |
| D. | 225.5 : 452.8 |
| Answer» D. 225.5 : 452.8 | |
| 41. |
The K |
| A. | 80 or 30 |
| B. | 100 or 40 |
| C. | 90 or 10 |
| D. | 60 or 100 |
| Answer» D. 60 or 100 | |
| 42. |
Which one of the following graphs represents uncompetitive inhibition ? |
| A. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-9A.png"> |
| B. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-9B.png"> |
| C. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-9C.png"> |
| D. | <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-9D.png"> |
| Answer» B. <img src="http://images.interviewmania.com/wp-content/uploads/2019/12/Q-9B.png"> | |
| 43. |
A single subunit enzyme converts 420 moles of substrate to product in one minute. The activity of the enzyme is ______ 10 |
| A. | 1 |
| B. | 3 |
| C. | 5 |
| D. | 7 |
| Answer» E. | |
| 44. |
An enzyme is immobilized on the surface of a non-porous spherical particle of 2 mm diameter. The immobilized enzyme is suspended in a solution having bulk substrate concentration of 10 mM. The enzyme follows first order kinetics with rate constant 10 s |
| A. | 8.5 : 8.5 |
| B. | 7.5 : 7.5 |
| C. | 5.5 : 5.5 |
| D. | 2.5 : 2.5 |
| Answer» C. 5.5 : 5.5 | |
| 45. |
In an assay of the type II dehydroquinase of molecular mass 18 kDa, it is found that the V |
| A. | 7.5 : 10.05 |
| B. | 8.5 : 8.9 |
| C. | 10.85: 14.89 |
| D. | 8.6 : 9.4 |
| Answer» E. | |
| 46. |
Choose the CORRECT combination of True (T) and False (F) statements about microcarriers used in animal cell culture. |
| A. | P-T, Q-F, R-T and S-F |
| B. | P-T, Q-T, R-F and S-F |
| C. | P-F, Q-F, R-T and S-T |
| D. | P-F, Q-T, R-F and S-T |
| Answer» C. P-F, Q-F, R-T and S-T | |
| 47. |
Identify the enzyme that catalyzes the following reaction |
| A. | Glutamate synthetase |
| B. | Glutamate oxoglutarate aminotransferase |
| C. | Glutamate dehydrogenase |
| D. | -ketoglutarate deaminase |
| Answer» D. -ketoglutarate deaminase | |
| 48. |
The turnover numbers for the enzymes, E1 and E2 are 150 s |
| A. | E1 binds to its substrate with higher affinity than E2 |
| B. | The velocity of reactions catalyzed by E1 and E2 at their respective saturating substrate concentrations could be equal, if concentration of E2 used is 10 times that of E1 |
| C. | The velocity of E1 catalyzed reaction is always greater than that of E2 |
| D. | The velocity of E1 catalyzed reaction at a particular enzyme concentration and saturating substrate concentration is lower than that of E2 catalyzed reaction under the same conditions |
| Answer» C. The velocity of E1 catalyzed reaction is always greater than that of E2 | |
| 49. |
An immobilized enzyme being used in a continuous plug flow reactor exhibits an effectiveness factor ( ) of 1.2. The value of being greater than 1.0 could be apparently due to |
| A. | substrate inhibited with internal pore diffusion limitation |
| B. | external pore diffusion limitation |
| C. | sigmoidal kinetics |
| D. | unstability of the enzyme |
| E. | None of these |
| Answer» F. | |
| 50. |
The degree of inhibition for an enzyme catalyzed reaction at a particular inhibitor concentration is independent of initial substrate concentration. The inhibition follows |
| A. | competitive inhibition |
| B. | mixed inhibition |
| C. | un-competitive inhibition |
| D. | non-competitive inhibition |
| Answer» E. | |