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Enzymic resolution of dl-phenylglycine

Paper ID Volume ID Publish Year Pages File Format Full-Text
36643 45139 2005 4 PDF Available
Title
Enzymic resolution of dl-phenylglycine
Abstract

An enzymic process of production of d- and l-phenylglycine is described. The unnatural amino acid dl-phenylglycine was synthesized from benzaldehyde and its dl-N-acetyl derivative obtained. Hog kidney acylase I, an amidohydrolase, was used as catalyst to hydrolyse enantiospecifically with 100% conversion of l-N-acetylphenylglycine. l-Phenylglycine was obtained with 36% isolated yield, with over 99% of enantiomeric excess. After acid hydrolysis using 48% HBr (v/v), unreacted d-N-acetylphenylglycine, yielded d-phenylglycine in 26% isolated yield, with over 95% of enantiomeric excess. The present methodology constitutes a new preparative route to produce both enantiomers of phenylglycine and is suitable for industrial use.

Keywords
Enantiomeric resolution; dl-N-Acetylphenylglycine; l-Phenylglycine; d-Phenylglycine; Acylase I; Ion exchange chromatography
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 10, October 2005, Pages 3186–3189
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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