Purification and Characterization of L-Phenylalanine Aminopeptidase from Chick-Pea Cotyledons (Cicer arietinum L.)

Title: Purification and Characterization of L-Phenylalanine Aminopeptidase from Chick-Pea Cotyledons (Cicer arietinum L.)

Volume: 16 Issue: 2

Author(s): Margarita Marinova, Alexander Dolashki, Florian Altenberend, Stefan Stevanovic, Wolfgang Voelter and Bozhidar Tchorbanov

Affiliation:

Keywords: Chick-pea cotyledons, aminopeptidase, kinetic analysis, antihypertensive peptides

Abstract: Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase – 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and 35-40°C. The determined constant of specificity kcat/Km during hydrolysis of Nunsubstituted amino acid-p-nitroanilides showed a decrease order: Phe > Leu > Pro > Ile > Val > Ala. The enzyme was strongly inhibited by p-chloromercuribenzoic acid as well as in a competitive rate by the antihypertensive peptides Ile-Pro-Pro and Val-Pro-Pro.

Cite this article as:

Marinova Margarita, Dolashki Alexander, Altenberend Florian, Stevanovic Stefan, Voelter Wolfgang and Tchorbanov Bozhidar, Purification and Characterization of L-Phenylalanine Aminopeptidase from Chick-Pea Cotyledons (Cicer arietinum L.), Protein & Peptide Letters 2009; 16 (2) . https://dx.doi.org/10.2174/092986609787316333