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Applied and Environmental Microbiology, February 2003, p. 1246-1250, Vol. 69, No. 2
0099-2240/03/$08.00+0 DOI: 10.1128/AEM.69.2.1246-1250.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Laboratory of Microbiology, Wageningen University, 6703 HA Wageningen ,1 DSM Food Specialties, 2600 MA Delft, The Netherlands2
Received 1 July 2002/ Accepted 5 November 2002
A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards phenylalanine ß-naphthylamide (F-ßNA) and phenylalanine para-nitroanilide (F-pNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to ßNA; other amino acids with nonaromatic side chains coupled to either pNA or ßNA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases.
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