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Enzyme-assisted Preparation of D-tert.-Leucine
Author(s) -
Kurt Laumen,
Oreste Ghisalba,
Kurt Auer
Publication year - 2001
Publication title -
bioscience biotechnology and biochemistry
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.65.1977
Subject(s) - saponification , bacillus licheniformis , hydrolysis , chemistry , leucine , enzyme , protease , monomer , ethyl ester , organic chemistry , chromatography , biochemistry , amino acid , bacteria , bacillus subtilis , polymer , biology , genetics
Optically pure D-tert.-leucine was obtained by the enzymatic hydrolysis of (+/-)-N-acetyl-tert. leucine chloroethyl ester after about 50% conversion, this being catalyzed by a protease from Bacillus licheniformis (Alcalase), and subsequent acidic saponification of the recovered ester. Among the methyl, ethyl, octyl, chloroethyl and trichloroethyl esters, the chloroethyl ester exhibited the highest rate of hydrolysis.

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