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Purification and characterization of aminopeptidase N from chicken intestine with potential application in debittering

Paper ID Volume ID Publish Year Pages File Format Full-Text
35625 45098 2010 6 PDF Available
Title
Purification and characterization of aminopeptidase N from chicken intestine with potential application in debittering
Abstract

An aminopeptidase with broad substrate specificity was purified to homogeneity (123.7-fold) with a yield of 3.43% from chicken (Gallus gallus) intestine using a combination of chromatographic separation strategies. The enzyme was identified as alanyl aminopeptidase or aminopeptidase N (APN) by Peptide Mass Fingerprinting. The molecular weight of the enzyme was estimated to be ∼180 kDa by SDS-PAGE and gel filtration chromatography. The enzyme was found to be a glycoprotein, having 40% sugar residue and a molecular mass of 108 kDa after deglycosylation. The enzymatic activity was optimal at 60 °C and pH 6.0. The enzyme preferentially hydrolyzed Leu-β-NA (Km = 0.1 mM) followed by Ala, Phe, Tyr and Gly at N-terminal. The enzyme activity was completely inhibited by 1,10 phenanthroline (1 mM) and bestatin (1 mM) confirming it as a metalloprotease. Potential of this enzyme in combination with other endoproteases for the production of debittered protein hydrolysates has been discussed.

Keywords
APN; Chicken; Glycoprotein; Intestine; Aminopeptidase; Leu-β-NA
First Page Preview
Purification and characterization of aminopeptidase N from chicken intestine with potential application in debittering
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 6, June 2010, Pages 1011–1016
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering