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

Abstract：

:An extracellular α-galactosidase (Gal27A) with high specific activity of 423Umg(-1) was identified in thermophilic Neosartorya fischeri P1. Its coding gene (1680bp) was cloned and functionally expressed in Pichia pastoris. Sequence analysis indicated that deduced Gal27A contains a catalytic domain of glycoside hydrolase family 27. The native and recombinant enzymes shared some similar properties, such as pH optima at 4.5, temperature optima at 60-70°C, resistance to most chemicals and saccharides, and great abilities to degrade raffinose and stachyose in soymilk. Considering the high yield (3.1gL(-1)) in P. pastoris, recombinant rGal27A is more favorable for industrial applications. This is the first report on purification and gene cloning of Neosartorya α-galactosidase.

journal_name

Bioresour Technol

journal_title

Bioresource technology

authors

Wang H,Shi P,Luo H,Huang H,Yang P,Yao B

doi

10.1016/j.biortech.2013.11.078

subject

Has Abstract

pub_date

2014-02-01 00:00:00

pages

361-4

eissn

0960-8524

issn

1873-2976

pii

S0960-8524(13)01804-X

journal_volume

153

pub_type

杂志文章

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