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Summary: Monatshefte fuÈr Chemie 131, 667±672 (2000)
Beauveria bassiana ATCC 7159 Contains
an L-Speci®c a-Amino Acid Benzamidase
Herbert L. HollandÃ, Peter R. Andreana, Reza Salehzadeh-Asl,
Aaron van Vliet, Nancy J. Ihasz, and Frances M. Brown
Institute of Molecular Catalysis, Department of Chemistry, Brock University, St. Catharines, ON
L2S 3A1, Canada
Summary. Biotransformation of a series of racemic N-benzoyl -amino acids by the fungus
Beauveria bassiana ATCC 7159 results in isolation of the corresponding D-amino acid benzamides
in high enantiomeric purity and yield.
Keywords. Amino acid; Beauveria bassiana; Biocatalysis; Biotransformation, Kinetic resolution
Introduction
Enzymatic methods for the kinetic resolution of racemic -amino acids are well
established [1]. Methods have been developed that involve the stereoselective
hydrolysis of carboxylic acid ester [2] or amino amide [3] derivatives; either D- or
L-speci®c hydrolysis can occur, and the product may be isolated as the free amino
acid or as the unhydrolyzed substrate [4]. These transformations are summarized in
Fig. 1.
Enantioselective hydrolyses involving amide derivatives of the amino group are
most frequently reported using an amino acylase enzyme preparation [5] or a whole
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