Stopped-flow kinetic studies of the cellulase-catalyzed conversion of cellulose to glucose.

Abstract:

:The kinetics of the cellulase-catalyzed conversion of soluble cellulose into glucose have been studied over a range of substrate concentrations and temperatures, and at pH values ranging from 4.75 to 7.0. Lineweaver-Burk plots were linear and led to V = 6.2muM/s and K(m) = 13.1 mM at pH 5.8 and 25.0 degrees C. The pK values corresponding to the free enzyme are 4.8 and 6.8 and are consistent with carboxyl and imidazole groups as the active ionizing species. These pK values were little changed in the enzyme-substrate intermediate that reacts in the ratedetermining step, suggesting that the ionizing groups are still free in this intermediate. The activation energy corresponding to V/K(m) is 80.6 kJ/mol, and that corresponding to V is 38.7 kJ/mol. The corresponding entropies of activation are 21 J K(-1) mol(-1) and -157 J K(-1) mol(-1), respectively.

journal_name

Biotechnol Bioeng

authors

Banerjee DK,Laidler KJ

doi

10.1002/bit.260251011

subject

Has Abstract

pub_date

1983-10-01 00:00:00

pages

2413-8

issue

10

eissn

0006-3592

issn

1097-0290

journal_volume

25

pub_type

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