Enzyme-assisted Preparation of D-tert.-Leucine

Article abstract of DOI:10.1271/bbb.65.1977

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.

Full text of DOI:10.1271/bbb.65.1977

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Bioscience, Biotechnology, and Biochemistry
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Enzyme-assisted Preparation of D-tert.-Leucine
Kurt LAUMENa, Oreste GHISALBAa & Kurt AUERa
a Novartis Pharma AG, Core Technology Area
Published online: 22 May 2014.
To cite this article: Kurt LAUMEN, Oreste GHISALBA & Kurt AUER (2001) Enzyme-assisted Preparation of D-tert.-Leucine,
Bioscience, Biotechnology, and Biochemistry, 65:9, 1977-1980, DOI: 10.1271/bbb.65.1977
To link to this article: http://dx.doi.org/10.1271/bbb.65.1977
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