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

^*この研究の対応する著者

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月 6

ASJC Scopus subject areas

バイオテクノロジー
分析化学
生化学
応用微生物学とバイオテクノロジー
分子生物学
有機化学

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abstract = "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).",

keywords = "Maltose phosphorylase, Transglycosylation, α-glucoside",

author = "Kuniki Kino and Yu Shimizu and Shoko Kuratsu and Kohtaro Kirimura",

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doi = "10.1271/bbb.70117",

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T1 - Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase

AU - Kino, Kuniki

AU - Shimizu, Yu

AU - Kuratsu, Shoko

AU - Kirimura, Kohtaro

PY - 2007/7/6

Y1 - 2007/7/6

N2 - 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).

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).

KW - Maltose phosphorylase

KW - Transglycosylation

KW - α-glucoside

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DO - 10.1271/bbb.70117

M3 - Article

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AN - SCOPUS:34347338778

VL - 71

SP - 1598

EP - 1600

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 6

ER -

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

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