Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase
2007
Kino, K.(Waseda Univ., Tokyo (Japan)) | Kuratsu, S. | Kirimura, K.
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-alpha-D-glucopyranoside (alpha-SalGlc) was identified. The yield based on supplied salicyl alcohol was 86% (mol/mol).
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书目信息
页码
pp. 1598-1600
其它主题
Proteinas recombinantes; Biosintesis; Proteine recombinante
语言
英语
注释
Summary (En)
1 tab. 2 fig. 11 ref.
类型
Summary
2008-05-15
AGRIS AP