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Enzymatic synthesis of a novel trehalose derivative, 3,3′‐diketotrehalose, and its potential application as the trehalase enzyme inhibitor
Author(s) -
Sode Koji,
Akaike Eri,
Sugiura Hiroto,
Tsugawa Wakako
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02427-3
Subject(s) - trehalase , trehalose , maltase , enzyme , chemistry , biochemistry , dehydrogenase , derivative (finance) , hydrolysis , financial economics , economics
We reported the preparation of a novel trehalose derivative based on enzymatic oxidation of trehalose by water‐soluble glucose‐3‐dehydrogenase (G3DH) from marine bacterium Halomonas sp. α‐15 cells. The product of G3DH enzymatic conversion was 3,3′‐diketotrehalose (3,3′dkT), a novel trehalose derivative of which both third hydroxy groups of glucopyranosides were oxidized. 3,3′dkT was revealed to show an inhibitory effect toward pig‐kidney and Bombyx mori trehalases. The IC 50 values of 3,3′dkT were 0.8 and 2.5 mM and K i values were 0.2 and 0.6 mM for pig‐kidney and for B. mori trehalases, respectively. In addition, 3,3′dkT did not show any inhibitory effect on both maltase and mannosidase activities. Therefore, 3,3′dkT was a specific inhibitor of trehalases.