Catalane in un enzyme that speeds up the decomposition ot hydrogen peroxide H0) to waler and axvgen.Students conducted two investigationa to determine the ideal conditions for the function of catalane. Onewetigation compared catalase activity at diferent values of pH. The other imvestigation compared catalaneactivity al diferent temperatures.Enayme Activityve pHEnzyme Aetivityvs TemperatureTeate C)According to the data in the graphs, which pH and temperature combination provides the BEST conditions forcatalase to tunction?Anurylag a

Enzymes are biocatalyst which binds to the substrate and stabilizes the high energy transition state…

Answered: Catalane in un enzyme that speeds up…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-
It is required to recover active extracellular enzymes from a completed fermentation mediumthat also consists of proteins (<200,000 molecular weight cut-off (MWCO)) and bacterial cells (1-2μm). A cross-flow 0.35 μm microfiltration (MF) with retentate recycled back to the fermenter willbe used over a period of 5 hours during which time flux is assumed to decline linearly. After 5 hours, assuming 95% of the bacteria are retained and given the additionalinformation below, what is the concertation of bacteria remaining in the fermenter and what area,in m2 , of MF membrane is needed? Initial bacterial concentration = 1.2 gdcw /L (dcw = dry cell weight)Volume of medium at the beginning = 15 m3Volume of medium left in the fermenter after 5 hours filtering = 1 m3Initial (starting flux) = 6.5 x 10-5 m sec -1Final flux (after 5 hours of filtering) = 3.9 x 10-5 m sec -
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The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?

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