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  • Title: A thermophilic α-galactosidase from Neosartorya fischeri P1 with high specific activity, broad substrate specificity and significant hydrolysis ability of soymilk.
    Author: Wang H, Shi P, Luo H, Huang H, Yang P, Yao B.
    Journal: Bioresour Technol; 2014 Feb; 153():361-4. PubMed ID: 24360500.
    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.
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