Enhancement of enantioselectivity in the Bacillus subtilis protease-catalyzed hydrolysis of N-free amino acid esters using the ester grouping-modification approach

The generality of enantioselectivity enhancement through the modification of the alcohol moiety of a substrate ester was ascertained, for in the Bacillus subtilis protease-catalyzed hydrolysis of N-unprotected amino acid esters the enantioselectivity was enhanced largely by switching the conventiona...

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Bibliographic Details
Published in:Biotechnology letters 2006-03, Vol.28 (5), p.295-299
Main Authors: MIYAZAWA, Toshifumi, MINOWA, Hiroe, YAMADA, Takashi
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - chemistry
Aspergillus oryzae
Aspergillus oryzae - enzymology
Bacillus subtilis
Bacillus subtilis - enzymology
Bacteria
Bacteriology
Biological and medical sciences
Biotechnology
Catalysis
Enzyme Activation
Esters
Fundamental and applied biological sciences. Psychology
Hydrolysis
Peptide Hydrolases - chemistry
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Summary:The generality of enantioselectivity enhancement through the modification of the alcohol moiety of a substrate ester was ascertained, for in the Bacillus subtilis protease-catalyzed hydrolysis of N-unprotected amino acid esters the enantioselectivity was enhanced largely by switching the conventional methyl ester to esters with a longer alkyl chain such as the isobutyl ester (from E = 3 to E = 130-170 in the case of 4-fluorophenylalanine esters) as in the enzymatic hydrolysis mediated by Aspergillus oryzae protease. There was indeed a profound dependence of E on the nature of the ester grouping.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-005-5713-y