Two neutral thermostable cellulases from Phialophora sp. G5 act synergistically in the hydrolysis of filter paper.

Authors :: Zhao J
Shi P
Li Z
Yang P
Luo H
Bai Y
Wang Y
Yao B
Source :: Bioresource technology [Bioresour Technol] 2012 Oct; Vol. 121, pp. 404-10. Date of Electronic Publication: 2012 Jul 20.
Publication Year :: 2012
Abstract: Two novel cellulase genes, cbh6A and egGH45, were cloned from Phialophora sp. G5 and successfully expressed in Pichia pastoris. The putative polypeptide of CBH6A consists of a family 1 CBM and a catalytic domain of glycosyl hydrolase family 6 cellobiohydrolases, while deduced EgGH45 only contains a catalytic domain of family 45 endoglucanases. CBH6A and EgGH45 were optimally active at pH 7.0 and 65°C, and pH 6.0 and 60°C, respectively. Both enzymes exhibited high activities and stabilities over a wide pH range and had good thermostability at 70°C. CBH6A and EgGH45 had significant resistance to SDS (10mM), remaining 35% and 54% activities, respectively. These enzymes had synergic effect on the hydrolysis of filter paper, showing the highest efficiency in the ratio of CBH6A to EgGH45 at 80:20. The properties make this enzyme combination potential for application in textile and detergents industries.<br /> (Copyright © 2012 Elsevier Ltd. All rights reserved.)

Subjects :: Base Sequence
Cloning, Molecular
Computational Biology
Electrophoresis, Polyacrylamide Gel
Filtration instrumentation
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Molecular Sequence Data
Pichia
Protein Structure, Tertiary
Reverse Transcriptase Polymerase Chain Reaction
Sequence Analysis, DNA
Substrate Specificity
Temperature
Cellulases genetics
Cellulases metabolism
Paper
Phialophora enzymology

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