Novel serine penicillocarboxypeptidase CPD-S3 from Penicillium janthinellum IBT 3991: Purification, characterization, and uses in peptide synthesis and modification |
| |
Authors: | Estera Szwajcer Dey and Stig Aasmul-Olsen |
| |
Institution: | * Carlsberg Research Laboratory, Valby, Denmark ? Department of Research, Carlbiotech Ltd. A/S, Copenhagen, Denmark |
| |
Abstract: | A novel carboxypeptidase (CPD-S3) from Penicillium janthinellum IBT 3991 has been isolated in a two-step purification procedure by cation exchange and affinity chromatography. The enzyme is a serine carboxypeptidase with a denatured molecular mass determined by SDS of 62 kDa of which 32% is carbohydrate. The isoelectric point is 5.1. CPD-S3 exhibits a high stability towards organic solvents and elevated temperatures. Besides the carboxypeptidase activity, CPD-S3 exhibits esterase, amidase, and carboxamidohydrolase activities. CPD-S3 favors substrates of
-configuration with basic amino acid residues in either P1 or P1', and particularly dibasic substrates and medium-sized straight-chain alkyl esters for hydrolysis. In aminolysis of esters, amino acid amides and hydrazines coupled in good yield, but methyl esters poorly, and unlike other carboxypeptidases, free amino acids could not be coupled or transpeptidation effected to form amides. In ester semisynthesis, peptides with neutral, but not basic, residues in P1 could be esterified. The scope of applicability for enzymatic peptide synthesis is limited. |
| |
Keywords: | Fungal extracellular serine carboxypeptidase enzymatic hydrolysis and synthesis of peptides esters amides |
本文献已被 ScienceDirect 等数据库收录! |
|