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

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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).

Original language	English
Pages (from-to)	1598-1600
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	71
Issue number	6
DOIs	https://doi.org/10.1271/bbb.70117
Publication status	Published - 2007 Jul 6

Keywords

Maltose phosphorylase
Transglycosylation
α-glucoside

ASJC Scopus subject areas

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

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10.1271/bbb.70117

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title = "Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase",

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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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

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AN - SCOPUS:34347338778

SN - 0916-8451

VL - 71

SP - 1598

EP - 1600

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 6

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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