期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 80, 期 8, 页码 1562-1567出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2016.1182852
关键词
GH31; dextran; isomaltose; glucosyltransferase; Flavobacterium johnsoniae
类别
资金
- Japan Society for the Promotion of Science [26660277]
- Grants-in-Aid for Scientific Research [26660277] Funding Source: KAKEN
Glycoside hydrolase family (GH) 31 enzymes exhibit various substrate specificities, although the majority of members are -glucosidases. Here, we constructed a heterologous expression system of a GH31 enzyme, Fjoh_4430, from Flavobacterium johnsoniae NBRC 14942, using Escherichia coli, and characterized its enzymatic properties. The enzyme hydrolyzed dextran and pullulan to produce isomaltooligosaccharides and isopanose, respectively. When isomaltose was used as a substrate, the enzyme catalyzed disproportionation to form isomaltooligosaccharides. The enzyme also acted, albeit inefficiently, on p-nitrophenyl -D-glucopyranoside, and p-nitrophenyl -isomaltoside was the main product of the reaction. In contrast, Fjoh_4430 did not act on trehalose, kojibiose, nigerose, maltose, maltotriose, or soluble starch. The optimal pH and temperature were pH6.0 and 60 degrees C, respectively. Our results indicate that Fjoh_4430 is a novel GH31 dextranase with high transglucosylation activity.
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