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Biotechnology Engineering

Bioprocess Engineering And Process Biotechnology MCQs

Practice Bioprocess Engineering And Process Biotechnology MCQs for competitive exams.

Bioprocess Engineering And Process Biotechnology MCQs

Practice questions from this topic.

Match the entries in Group I with the process parameters in Group II . Group I Group II P. Clark electrode 1. Liquid level Q. Redox probe 2. Dissolved oxygen concentration R. Load cell 3. Vessel pressure S. Diaphragm gauge 4. pH (anaerobic process)

  1. A. P-2, Q-1, R-3, S-4
  2. B. P-4, Q-2, R-3, S-1
  3. C. P-2, Q-4, R-1, S-3
  4. D. P-2, Q-1, R-4, S-3
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Phytase, an enzyme produced by Aspergillus niger can be adsorbed on microcrystalline cellulose powder (MCCP). The adsorption follows a Langmuir isotherm and the maximum concentration of the protein that can be obtained on the adsorbent is 70 mg cm -1 . At a concentration of 50 mg L -1 of protein in the solution, the concentration of protein on the adsorbent reaches 35 mg cm -1 . It is desired to recover 90% of the protein from 1.5 liter of the cell free culture filtrate containing 220 mg L -1 protein by addition of MCCP to the solution. The concentration of the protein adsorbed on the solid at equilibrium will be:

  1. A. 21.4 mg cm -3
  2. B. 214 mg cm -3
  3. C. 2.14 mg cm -3
  4. D. None of the above
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In large-scale fermentation, the preferred method of sterilization is

  1. A. Chemicals
  2. B. Radiation
  3. C. Filtration
  4. D. Heat
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In large scale fermentation process, air is sterilized by

  1. A. Jute fiber
  2. B. Membrane
  3. C. Cotton fiber
  4. D. Glass wool fiber
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If the dissociation constant for solute-adsorbent binding is K D , the retention time of the solute in a chromatography column

  1. A. Increases with increasing K D
  2. B. Decreases with increasing K D
  3. C. Passes through minimum with increasing K D
  4. D. Is independent of K D
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An immobilized enzyme being used in a continuous plug flow reactor exhibits an effectiveness factor (η) of 1.2. The value of η being greater than one could be apparently due to one of the following reasons. Identify the correct reason.

  1. A. The enzyme follows substrate inhibited kinetics with internal pore diffusion limitation
  2. B. The enzymes experiences external film diffusion limitation
  3. C. The enzyme follows sigmoidal kinetics
  4. D. The immobilized enzyme is operationally unstable
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Which of the following techniques is not ideal for immobilizing cell-free enzymes?

  1. A. Physical entrapment by encapsulation
  2. B. Covalent chemical bonding to surface carriers
  3. C. Physical bonding by flocculation
  4. D. Covalent chemical bonding by cross-linking the precipitate
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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.

  1. A. P, Q
  2. B. R, S
  3. C. P, S
  4. D. Q, S
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The specific growth rate (μ) of a microorganism in death phase is

  1. A. 0 (zero)
  2. B. μ max
  3. C. Less than zero
  4. D. Greater than zero
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Aeration in a bioreactor is provided by

  1. A. Impeller
  2. B. Baffles
  3. C. Sparger
  4. D. All of the above
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Two monomeric His-tagged proteins of identical molecular weight are present in a solution. pIs of these two proteins are 5.6 and 6.8. Which one of the following techniques can be used to separate them?

  1. A. Denaturing polyacrylamide gel electrophoresis
  2. B. Size-exclusion chromatography
  3. C. Ion-exchange chromatography
  4. D. Nickel affinity chromatography
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Downstream processing of an industrial process yielded a highly purified bioactive protein. This protein was subjected to cleavage by trypsin. Chromatographic separation of products resulted in 4 peptides (P, Q, R, S) with the following amino acid sequences. P. Phe-Val-Met-Val-Arg Q. Ala-Ala-Try-Gly-Lys R. Val-Phe-Met-Ala-Gly-Lys S. Phe-Gly-Try-Ser-Thr Chemical cleavage of the same protein with cyanogen bromide and chromatographic separation resulted in three peptides (i, ii, iii) with the following sequences (i) Ala-Gly-Lys-Phe-Gly-Try-Ser-Thr (ii) Ala-Ala-Try-Gly-Lys-Phe-Val-Met (iii) Val-Arg-Val-Phe-Met The order of the peptides that gives the primary structure of the original protein is

  1. A. P, Q, R, S
  2. B. Q, P, R, S
  3. C. Q, R, P, S
  4. D. R, Q, P, S
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