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Kino, K. et al.

Kuniki Kino, Yu Shimizu, Shoko Kuratsu, Kohtaro Kirimura,

Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase.

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).[1]

References

Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase. Kino, K., Shimizu, Y., Kuratsu, S., Kirimura, K. Biosci. Biotechnol. Biochem. (2007) [Pubmed]

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