In:
Journal of Chemistry, Hindawi Limited, Vol. 2018 ( 2018-12-17), p. 1-8
Abstract:
In this study, α -glucanotransferase from Bacteroides thetaiotaomicron was expressed in Escherichia coli and characterized. Conserved amino-acid sequence alignment showed that Bacteroides thetaiotaomicron α -glucanotransferase (Bt α GTase) belongs to the glycoside hydrolase family 77. The enzyme exhibited optimal catalytic activity at 60°C and pH 3.0. Bt α GTase catalyzed transglycosylation reactions that produced only glycosyl or maltosyl transfer products, which are preferable for the generation of transglycosylated products with high yield. The 1-deoxynojirimycin (DNJ) glycosylation product G1-DNJ was generated using Bt α GTase, and the inhibitory effect of G1-DNJ was analyzed. A kinetic study of inhibition revealed that G1-DNJ inhibited α -glucosidase to a greater extent than did DNJ but did not show any inhibitory effects towards α -amylase, suggesting that G1-DNJ is a potential candidate for the prevention of diabetes.
Type of Medium:
Online Resource
ISSN:
2090-9063
,
2090-9071
DOI:
10.1155/2018/2981596
Language:
English
Publisher:
Hindawi Limited
Publication Date:
2018
detail.hit.zdb_id:
2393625-3
detail.hit.zdb_id:
2703077-5
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