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Recent questions tagged kinetics

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GATE2018-53
Consider a simple uni-substrate enzyme that follows Michaelis-Menten kinetics. When the enzyme catalyzed reaction was carried out in the presence of $10$ nM concentration of an inhibitor, there was no change in the maximal velocity. However. the slope of the Lineweaver-Burk plot increased $3$-fold. The dissociation constant for the enzyme-inhibitor complex (in nM) is ____________

gatecse asked in Biochemistry Feb 20, 2018

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GATE2018-52
First order deactivation rate constants for soluble and immobilized amyloglucosidase enzyme are $0.03 \text{ min}^{-1}$ and $0.005 \text{ min}^{-1}$, respectively. The ratio of half-life of the immobilized enzyme to that of the soluble enzyme is (rounded off to the nearest integer) ___________

gatecse asked in Biochemistry Feb 20, 2018

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GATE2018-47
In a chemostat, the feed flow rate and culture volume are $100$ ml/h and $1.0$ L, respectively. With glucose as substrate, the values of $\mu_{\text{max}}$ and $K_s$ are $0.2 \: h^{-1}$ and $1 \: g/L$, respectively. For a glucose concentration of $10 \: g/L$ in the feed, the effluent substrate concentration (in $g/L$) is _______

gatecse asked in Biochemistry Feb 20, 2018

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