Enhanced hydrolysis of soluble cellulosic substrates by a metallocellulase with veratryl alcohol-oxidase activity
Conference
·
OSTI ID:150410
- Oak Ridge National Lab., TN (United States)
A cellulose enzyme fraction was separated from Trichoderma reesei Pulpzyme HA{trademark}, and its characteristics suggested that it was mainly composed of cellobiohydrolase II (CBH II). The covalent attachment of pentaammineruthenium (III) to this enzyme resulted in threefold and fourfold enhancements of its hydrolytic activity on carboxymethyl cellulose (CMC) and barley {beta}-glucan, respectively, as well as endowing it with veratryl alcohol-oxidase activity. Enhancement of hydrolysis was not affected by addition of tartrate or hydrogen peroxide to the reaction mixture. Both native and pentaammineruthenium modified enzymes had negligible activity on cellobiose and p-nitrophenyl {beta}-cellobioside (PNPC).
- Research Organization:
- Oak Ridge National Lab., TN (United States)
- DOE Contract Number:
- AC05-84OR21400
- OSTI ID:
- 150410
- Report Number(s):
- CONF-940526--; CNN: Contract NAS7-918
- Country of Publication:
- United States
- Language:
- English
Similar Records
Enzyme kinetics by
GH7
cellobiohydrolases on chromogenic substrates is dictated by nonâproductive binding: insights from crystal structures and
MD
simulation
Journal Article
·
Mon Sep 05 20:00:00 EDT 2022
· Federation of European Biochemical Societies (FEBS) Journal
·
OSTI ID:1885622