Introduction
This quiz set on “Pharmaceutical applications of enzymes” is designed specifically for M.Pharm students pursuing Advanced Pharmaceutical Biotechnology. It covers core concepts such as enzyme therapeutics, immobilization techniques, enzyme-prodrug strategies, biosensors, formulation stability, and industrial enzyme use in drug manufacturing. Questions emphasize mechanistic understanding, practical applications in drug delivery and diagnostics, and considerations like enzyme kinetics, stability, and regulatory aspects. These MCQs will help reinforce classroom learning, prepare for exams, and support critical thinking about how enzymes are harnessed in modern pharmaceutical sciences for therapeutic, analytical, and manufacturing purposes.
Q1. Which characteristic of immobilized enzymes most directly improves their utility in continuous pharmaceutical production processes?
- Increased intrinsic catalytic turnover (kcat) of the enzyme
- Ease of enzyme recovery and reuse from the reaction stream
- Complete elimination of product inhibition
- Permanent alteration of enzyme amino acid sequence
Correct Answer: Ease of enzyme recovery and reuse from the reaction stream
Q2. Which enzyme is a clinically approved therapeutic for acute lymphoblastic leukemia due to its ability to deplete circulating asparagine?
- Uridine phosphorylase
- L-asparaginase
- N-acetylneuraminate lyase
- D-amino acid oxidase
Correct Answer: L-asparaginase
Q3. Which immobilization method provides covalent attachment and minimizes enzyme leaching but may risk partial activity loss due to modification?
- Encapsulation within alginate beads
- Covalent binding to activated supports (e.g., epoxy, glutaraldehyde)
- Physical adsorption on hydrophobic carriers
- Cross-linking enzyme aggregates without support (CLEAs)
Correct Answer: Covalent binding to activated supports (e.g., epoxy, glutaraldehyde)
Q4. In enzyme prodrug therapy, which statement describes the bystander effect?
- The enzyme-prodrug complex circulates unchanged to distant tissues
- Activated cytotoxic metabolite diffuses to kill neighboring cells not expressing the activating enzyme
- Immune cells remove activated drug molecules before they act
- Prodrug is excreted unchanged due to rapid renal clearance
Correct Answer: Activated cytotoxic metabolite diffuses to kill neighboring cells not expressing the activating enzyme
Q5. Which analytical application uses enzymes as recognition elements to detect glucose in blood samples?
- Enzyme replacement therapy
- Enzymatic biosensor (glucose oxidase-based)
- Prodrug activation assay
- Enzyme immobilization for continuous catalysis
Correct Answer: Enzymatic biosensor (glucose oxidase-based)
Q6. PEGylation of therapeutic enzymes primarily aims to:
- Increase substrate specificity of the enzyme
- Reduce immune recognition and prolong plasma half-life
- Enhance catalytic turnover (kcat) dramatically
- Convert the enzyme into a prodrug
Correct Answer: Reduce immune recognition and prolong plasma half-life
Q7. Which factor most strongly contributes to enzyme denaturation during formulation and storage of enzyme-based pharmaceuticals?
- Appropriate pH near the enzyme’s pI
- High ionic strength buffer optimized for activity
- Temperature excursions outside optimal stability range
- Use of stabilizing excipients like sugars
Correct Answer: Temperature excursions outside optimal stability range
Q8. Which enzyme class is most commonly targeted by statin drugs in cholesterol-lowering therapy?
- Serine proteases
- HMG-CoA reductase (a dehydrogenase enzyme)
- DNA topoisomerases
- Acetylcholinesterase
Correct Answer: HMG-CoA reductase (a dehydrogenase enzyme)
Q9. In the context of enzyme-based drug assays, Michaelis-Menten Km is important because it indicates:
- The maximum velocity achieved at infinite substrate concentration
- The substrate concentration at which reaction velocity is half-maximal, reflecting affinity
- The turnover number per enzyme molecule per second
- The rate constant for enzyme denaturation
Correct Answer: The substrate concentration at which reaction velocity is half-maximal, reflecting affinity
Q10. Which technique is most suitable for stabilizing enzymes against proteolytic degradation when used as biotherapeutics?
- Conjugation to polyethylene glycol (PEGylation)
- Encapsulation in immediate-release tablets
- Removal of glycosylation sites to reduce size
- Heating to high temperature before administration
Correct Answer: Conjugation to polyethylene glycol (PEGylation)
Q11. Which immobilization strategy is preferred when minimal mass-transfer limitation and easy substrate access are required for a soluble enzyme?
- Thick gel entrapment within high-density alginate
- Covalent linking inside nanoporous beads with very small pores
- Attachment as a thin layer on porous, high-surface-area carriers
- Cross-linking into large, dense aggregates
Correct Answer: Attachment as a thin layer on porous, high-surface-area carriers
Q12. Enzyme prodrugs activated by tumor-specific enzymes (e.g., MMPs) primarily aim to:
- Increase systemic toxicity to ensure tumor kill
- Localize cytotoxic activation to tumor microenvironment, reducing off-target effects
- Make drugs more hydrophilic for renal clearance
- Prevent drug penetration into tumor tissue
Correct Answer: Localize cytotoxic activation to tumor microenvironment, reducing off-target effects
Q13. Which property of lyophilized enzyme formulations most improves long-term stability for injectable enzyme therapeutics?
- High residual moisture content to retain flexibility
- Inclusion of stabilizers like sugars (trehalose, sucrose) and optimal pH
- Absence of any buffer to avoid ionic interactions
- Storage at room temperature regardless of product
Correct Answer: Inclusion of stabilizers like sugars (trehalose, sucrose) and optimal pH
Q14. Which statement best describes enzyme-linked immunosorbent assay (ELISA) application in pharmaceuticals?
- ELISA is used only for enzyme kinetic parameter determination
- ELISA employs enzymes conjugated to antibodies to detect and quantify antigens with high sensitivity
- ELISA replaces mass spectrometry for small-molecule quantification in all cases
- ELISA cannot be used for therapeutic drug monitoring
Correct Answer: ELISA employs enzymes conjugated to antibodies to detect and quantify antigens with high sensitivity
Q15. Which enzymatic modification strategy is commonly used to improve intestinal absorption of peptide drugs?
- Co-administration with broad-spectrum proteases
- Use of enzyme inhibitors (e.g., protease inhibitors) and permeation enhancers to protect peptides
- Deliberate removal of disulfide bonds to increase flexibility
- Formulation with high concentrations of free fatty acids to denature enzymes
Correct Answer: Use of enzyme inhibitors (e.g., protease inhibitors) and permeation enhancers to protect peptides
Q16. Which enzymatic diagnostic marker is measured to assess myocardial infarction (heart attack) in clinical practice?
- Amylase
- Creatine kinase-MB (CK-MB)
- Urease
- Lysozyme
Correct Answer: Creatine kinase-MB (CK-MB)
Q17. Which advantage do cross-linked enzyme aggregates (CLEAs) offer for pharmaceutical biocatalysis?
- They require large volumes of organic solvents for preparation
- CLEAs combine high enzyme loading, no carrier cost, and improved operational stability
- They are soluble and cannot be separated from product streams
- They universally eliminate all mass-transfer limitations
Correct Answer: CLEAs combine high enzyme loading, no carrier cost, and improved operational stability
Q18. Which mechanism explains reduced clearance of enzyme therapeutics after glycocalyx or glycan modification?
- Glycan removal leads to increased renal filtration
- Specific glycosylation patterns reduce recognition by hepatic clearance receptors (e.g., ASGPR)
- Glycan modification always increases immunogenicity and clearance
- Glycosylation converts enzymes into small peptides
Correct Answer: Specific glycosylation patterns reduce recognition by hepatic clearance receptors (e.g., ASGPR)
Q19. In enzyme immobilization for drug synthesis, which parameter must be optimized to balance activity and operational stability?
- pH of the storage buffer only, irrespective of reaction conditions
- The degree of multipoint attachment and spacer length between enzyme and support
- Complete denaturation to expose all active sites
- Using the largest possible particle size to avoid diffusion
Correct Answer: The degree of multipoint attachment and spacer length between enzyme and support
Q20. Which of the following best describes enzyme replacement therapy (ERT) for lysosomal storage diseases?
- Administration of small-molecule inhibitors to block substrate synthesis
- Periodic intravenous infusion of the missing or deficient enzyme to reduce substrate accumulation
- Use of broad-spectrum antibiotics to eliminate lysosomal bacteria
- Permanent cure by single oral dose of enzyme
Correct Answer: Periodic intravenous infusion of the missing or deficient enzyme to reduce substrate accumulation

I am a Registered Pharmacist under the Pharmacy Act, 1948, and the founder of PharmacyFreak.com. I hold a Bachelor of Pharmacy degree from Rungta College of Pharmaceutical Science and Research. With a strong academic foundation and practical knowledge, I am committed to providing accurate, easy-to-understand content to support pharmacy students and professionals. My aim is to make complex pharmaceutical concepts accessible and useful for real-world application.
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