期刊
BIOTECHNOLOGY LETTERS
卷 26, 期 23, 页码 1815-1819出版社
SPRINGER
DOI: 10.1007/s10529-004-5087-6
关键词
chloroperoxidase; enzyme stability; ionic liquid; stereoselectivity
Chloroperoxidase from Caldariomyces fumago catalyses the oxidation of 1,2-dihydronaphthalene to (1R,2R)-(+)-dihydroxytetrahydronaphthalene in homogenous citrate buffer/ionic liquid mixtures, using t-butyl hydroperoxide as 0) donor. It tolerates up to 30% (v/v) 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate. The enzyme activity in these ionic liquid co-solvent systems is retained for 24 h, but it falls to 3 h using non-ionic organic solvents such as t-BuOH or acetone.
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