⚗️ Biochemical Engineering Solved MCQs with Answers

Practice 513 approved ⚗️ Biochemical Engineering questions with verified answers from the 🧬 Medical Science subject for Pakistan exams.

513 solved MCQs

Which of these proteases is not a cysteine active site protease?Answer: Cathepsin D 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?Answer: A 10 fold increase in Vₘₐₓ would increase velocity 10 fold y The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained byAnswer: Induced fit The active site of an enzyme remainsAnswer: None of these Which category of enzymes belongs to class two in the international classification?Answer: Transferases 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 isAnswer: Significant The relationship between K(eq), Kₘ and Vₘₐₓ is known asAnswer: Haldane equation The reciprocal equation for non competitive inhibition can be arranged to the equation for theAnswer: Dixon plot Which of the following statements is true for enzymatically catalyzed reaction?Answer: The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it Which of the following common drugs is not a specific enzyme inhibitor?Answer: Iodine The enzyme inhibition can occur byAnswer: Both (a) and (b) In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?Answer: It changes the x-intercept Which of the following statements is not true?Answer: Enzymes only function when they are in intact cells Non-competitive inhibitor of an enzyme catalyzed reactionAnswer: Both (a) and (b) An enzyme and a reactant molecule maintain relationship asAnswer: A temporary association 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 isAnswer: 0.115 The plot commonly used for determining the value of Vₘₐₓ isAnswer: All of these Quasi steady state is also known asAnswer: All of these Which of these enzymes contains a Zinc (Zn) ion?Answer: Carboxypeptidase A A noncompetitive inhibitor of an enzyme-catalyzed reactionAnswer: Increases Kₘ and reduces Vₘₐₓ An allosteric inhibitor of an enzyme usuallyAnswer: Participates in feedback regulation Which of the following activity is possible by transferases?Answer: Both (a) and (b) A classical uncompetitive inhibitor is a compound that bindsAnswer: Reversibly to the enzyme substrate complex yielding an inactive ESI complex Which graphical method is used to determine an enzyme degree of cooperativity?Answer: Hill plot The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known asAnswer: Specific activity 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 asAnswer: (ν₀ - νᵢ)/ν₀ The rate equation in competitive inhibition based on Michaelis Menten equation is given byAnswer: rₘₐₓS/(Kₘ (1+I/Kᵢ)+S)) Classical noncompetitive inhibition is obtained only underAnswer: Rapid equilibrium conditions In the steady state the material balance equation for any component of a system isAnswer: Rate of addition - rate of removal + rate of formation = 0 For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vₘₐₓ) observed at [S] = 2 Kₘ will beAnswer: 0.66