首页|Altered substrate specificity of the gluco-oligosaccharide oxidase from Acremonium strictum

Altered substrate specificity of the gluco-oligosaccharide oxidase from Acremonium strictum

扫码查看
A gluco-oligosaccharide oxidase (GOOX) from Acremonium strictum type strain CBS 346.70 was cloned and expressed in Pichia pastoris. The recombinant protein, GOOX-VN, contained fifteen amino acid substitutions compared with the previously reported A. strictum GOOX. These two enzymes share 97% sequence identity; however, only GOOX-VN oxidized xylose, galactose, and N-acetylglucosamine. Besides monosaccharides, GOOX-VN oxidized xylo-oligosaccharides, including xylobiose and xylotriose with similar catalytic efficiency as for cello-oligosaccharides. Of three mutant enzymes that were created in GOOX-VN to improve substrate specificity, Y300A and Y300N doubled k_(cat) values for monosaccharide and oligosaccharide substrates. With this novel substrate specificity, GOOX-VN and its variants are particularly valuable for oxidative modification of cello- and xylo-oligosaccharides.

Acremonium strictumCarbohydrate dockingGluco-oligosaccharide oxidaseProtein engineeringSubstrate specificity

Vuong, T.V.、Master, E.R.、Foumani, M.

展开 >

Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada

2011

Biotechnology and Bioengineering

Biotechnology and Bioengineering

EISCI
ISSN:0006-3592
年,卷(期):2011.108(10)
  • 11
  • 26