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

Kuniki Kino, Yu Shimizu, Shoko Kuratsu, Kotaro Kirimura

    Research output: Contribution to journalArticle

    11 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 languageEnglish
    Pages (from-to)1598-1600
    Number of pages3
    JournalBioscience, Biotechnology and Biochemistry
    Volume71
    Issue number6
    DOIs
    Publication statusPublished - 2007

    Fingerprint

    maltose phosphorylase
    Maltose
    phosphorylase
    Glucosides
    maltose
    glucosides
    Alcohols
    alcohols
    Enterococcus hirae
    synthesis
    alcohol abuse
    Sugars
    sugars
    salicyl alcohol

    Keywords

    • α-glucoside
    • Maltose phosphorylase
    • Transglycosylation

    ASJC Scopus subject areas

    • Bioengineering
    • Biotechnology
    • Biochemistry
    • Biochemistry, Genetics and Molecular Biology(all)
    • Chemistry (miscellaneous)
    • Applied Microbiology and Biotechnology
    • Food Science

    Cite this

    Enzymatic synthesis of α-anomer-selective D-glucosides using maltose phosphorylase. / Kino, Kuniki; Shimizu, Yu; Kuratsu, Shoko; Kirimura, Kotaro.

    In: Bioscience, Biotechnology and Biochemistry, Vol. 71, No. 6, 2007, p. 1598-1600.

    Research output: Contribution to journalArticle

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