A thermophilic α-galactosidase from Neosartorya fischeri P1 with high specific activity, broad substrate specificity and significant hydrolysis ability of soymilk-Reference-Cited by-同舟云学术

A thermophilic α-galactosidase from Neosartorya fischeri P1 with high specific activity, broad substrate specificity and significant hydrolysis ability of soymilk

Published:2014-02 Issue: Volume:153 Page:361-364
ISSN:0960-8524
Container-title:Bioresource Technology
language:en
Short-container-title:Bioresource Technology

Author:

Wang Huimin,Shi Pengjun,Luo Huiying,Huang Huoqing,Yang Peilong,Yao Bin

Publisher

Elsevier BV

Subject

Waste Management and Disposal,Renewable Energy, Sustainability and the Environment,General Medicine,Environmental Engineering,Bioengineering

Reference15 articles.

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3. The carbohydrate-active enzymes database (CAZy): an expert resource for Glycogenomics;Cantarel;Nucleic Acids Res.,2009

4. Molecular cloning and expression of a novel protease-resistant GH-36 α-galactosidase from Rhizopus sp. F78 ACCC30795;Cao;J. Microbiol. Biotechnol.,2009

5. Expression of heterologpus proteins in Pichia pastoris: a useful experimental tool in protein engineering and production;Daly;J. Mol. Recognit.,2005

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