Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase

Kuniki Kino; Yu Shimizu; Shoko Kuratsu; Kohtaro Kirimura

doi:10.1271/bbb.70117

Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase

Kuniki Kino, Yu Shimizu, Shoko Kuratsu, Kohtaro Kirimura

先進理工学部

研究成果: Article › 査読

12 被引用数 (Scopus)

抄録

A maltose phosphorylase (EC 2.4.1.8; MPase) showed novel acceptor specificity and transferred the glucosyl moiety of maltose not only to sugars but also to various acceptors having alcoholic OH groups. Salicyl alcohol acted as acceptor for MPase from Enterococcus hirae, and the product, salicyl-O-α-D-glucopyranoside (α-SalGlc) was identified. The yield based on supplied salicyl alcohol was 86% (mol/mol).

本文言語	English
ページ（範囲）	1598-1600
ページ数	3
ジャーナル	Bioscience, Biotechnology and Biochemistry
巻	71
号	6
DOI	https://doi.org/10.1271/bbb.70117
出版ステータス	Published - 2007 7 6

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

文献へのアクセス

10.1271/bbb.70117

他のファイルとリンク

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引用スタイル

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AB - A maltose phosphorylase (EC 2.4.1.8; MPase) showed novel acceptor specificity and transferred the glucosyl moiety of maltose not only to sugars but also to various acceptors having alcoholic OH groups. Salicyl alcohol acted as acceptor for MPase from Enterococcus hirae, and the product, salicyl-O-α-D-glucopyranoside (α-SalGlc) was identified. The yield based on supplied salicyl alcohol was 86% (mol/mol).

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KW - Transglycosylation

KW - α-glucoside

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