Masters Theses

Abstract

"The entire time course of the hydrolysis of p-nitrophenyl-a-D-glucoside by the enzyme glucoamylase I was followed spectrophotometrically. Using time versus absorbance data the constants in the Michaelis-Menten equation were determined. The effect of the addition of product to the initial reaction mixture and the effect of solvent and temperature were determined. It was found that product produced during the reaction did not have the same effect upon the rate as did product added initially to the reaction mixture. The presence of substrate caused the enzyme to acquire protection against inhibition by the product"-- Abstract, p. ii

Advisor(s)

Poling, Bruce E.

Committee Member(s)

Crosser, Orrin K.
Siehr, Donald J.

Department(s)

Chemical and Biochemical Engineering

Degree Name

M.S. in Chemical Engineering

Publisher

University of Missouri--Rolla

Publication Date

1975

Pagination

vi, 40 pages

Note about bibliography

Includes bibliographical references (pages 36-37)

Rights

© 1975 Mark L. Dickhaus, All rights reserved.

Document Type

Thesis - Open Access

File Type

text

Language

English

Thesis Number

T 4059

Print OCLC #

5984420

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