Cross-linked enzyme aggregates of Mung bean epoxide hydrolases: a highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides.

TitleCross-linked enzyme aggregates of Mung bean epoxide hydrolases: a highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides.
Publication TypeJournal Article
Year of Publication2013
AuthorsYu C-Y, Li X-F, Lou W-Y, Zong M-H
JournalJournal of biotechnology
Volume166
Issue1-2
Pagination12-9
Date Published2013 Jun 20
Abstract

A highly active and stable cross-linked enzyme aggregates (CLEAs) of epoxide hydrolases (EHs) from Mung bean, which plays a crucial role in synthesis of valuable enantiopure diols, were successfully prepared and characterized. Under the optimum preparation conditions, the activity recovery of CLEAs recorded 92%. The CLEAs were more efficient than the free enzyme in catalyzing asymmetric hydrolysis of styrene oxide to (R)-1-phenyl-1,2-ethanediol in organic solvent-containing biphasic system. The biocatalytic reaction performed in n-hexane/buffer biphasic system had a clearly faster initial reaction rate, much higher product yield and product e.e. value than that in aqueous medium. Moreover, the optimal volume ratio of n-hexane to buffer, reaction temperature, buffer pH value and substrate concentration for the enzymatic hydrolysis were found to be 1:1, 40 °C, 7.5 and 30 mM, respectively, under which the initial reaction rate, product yield and product e.e. value were 13.26 mM/h, 46% and 93.5%, respectively. The CLEAs retained more than 50% of their initial activity after 8 batches of re-use in phosphate buffer and maintained 53% of their original activity after 8 reaction cycle in biphasic system. The efficient biocatalytic process with CLEAs proved to be feasible on a 250-mL preparative scale, exhibiting great potential for asymmetric synthesis of chiral diols.

DOI10.1155/2013/915213
Alternate JournalJ. Biotechnol.