Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima

Barbara R. Evans; Amanda K. Gilman; Kimberley Cordray; Jonathan Woodward

doi:10.1023/A:1005656203233

Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima

Barbara R. Evans, Amanda K. Gilman, Kimberley Cordray, Jonathan Woodward

Geochemistry & Interfacial Science

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

A cellulase from the thermophile, Thermotoga maritima, hydrolyzed oligosaccharide substrates by an exoglucanase mode of action but acted as an endoglucanase to rapidly reduce the viscosity of the soluble polysaccharides carboxymethylcellulose and barley β-glucan. The V(max) for hydrolysis of the substrate, p-nitrophenyl α-D-cellobioside, was 42 μmol min^-1 (mg protein)^-1, while that for barley β-glucan was 637. The enzyme had little activity on crystalline cellulose.

Original language	English
Pages (from-to)	735-740
Number of pages	6
Journal	Biotechnology Letters
Volume	22
Issue number	9
DOIs	https://doi.org/10.1023/A:1005656203233
State	Published - 2000

Funding

∗∗Managed by Lockheed Martin Energy Research Corp. for the US Department of Energy under contract DE-AC05-96OR22464. †The US Government right to retain a non-exclusive royalty-free license in and to any copyright is acknowledged.

Keywords

Cellulase
Hyperthermophile
Mechanism
Synergy

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title = "Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima",

abstract = "A cellulase from the thermophile, Thermotoga maritima, hydrolyzed oligosaccharide substrates by an exoglucanase mode of action but acted as an endoglucanase to rapidly reduce the viscosity of the soluble polysaccharides carboxymethylcellulose and barley β-glucan. The V(max) for hydrolysis of the substrate, p-nitrophenyl α-D-cellobioside, was 42 μmol min-1 (mg protein)-1, while that for barley β-glucan was 637. The enzyme had little activity on crystalline cellulose.",

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AU - Evans, Barbara R.

AU - Gilman, Amanda K.

AU - Cordray, Kimberley

AU - Woodward, Jonathan

PY - 2000

Y1 - 2000

N2 - A cellulase from the thermophile, Thermotoga maritima, hydrolyzed oligosaccharide substrates by an exoglucanase mode of action but acted as an endoglucanase to rapidly reduce the viscosity of the soluble polysaccharides carboxymethylcellulose and barley β-glucan. The V(max) for hydrolysis of the substrate, p-nitrophenyl α-D-cellobioside, was 42 μmol min-1 (mg protein)-1, while that for barley β-glucan was 637. The enzyme had little activity on crystalline cellulose.

AB - A cellulase from the thermophile, Thermotoga maritima, hydrolyzed oligosaccharide substrates by an exoglucanase mode of action but acted as an endoglucanase to rapidly reduce the viscosity of the soluble polysaccharides carboxymethylcellulose and barley β-glucan. The V(max) for hydrolysis of the substrate, p-nitrophenyl α-D-cellobioside, was 42 μmol min-1 (mg protein)-1, while that for barley β-glucan was 637. The enzyme had little activity on crystalline cellulose.

KW - Cellulase

KW - Hyperthermophile

KW - Mechanism

KW - Synergy

UR - http://www.scopus.com/inward/record.url?scp=0034047876&partnerID=8YFLogxK

U2 - 10.1023/A:1005656203233

DO - 10.1023/A:1005656203233

M3 - Article

AN - SCOPUS:0034047876

SN - 0141-5492

VL - 22

SP - 735

EP - 740

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 9

ER -

Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima

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