Bioactive Peptides from Bovine Milk α-Casein: Isolation, Characterization and Multifunctional properties

Article

Abstract

α-Casein group of proteins makes up to 65% of the total casein and consists of αS1- casein, αS2- casein and other related proteins. Among all the proteases employed, chymotryptic peptides showed maximum inhibition for angiotensin converting enzyme (ACE). The degree of hydrolysis and release kinetics of the peptides during chymotrypsin hydrolysis was compared with biological activity and the potent peptides fractions were identified. The crude fraction obtained after 110 min of hydrolysis shows multifunctional activities, like ACE inhibition, antioxidant activity, prolyl endopeptidase inhibitory activity and antimicrobial activities. This fraction was further purified by HPLC and sequenced by mass spectra. This fraction constituted peptides with molecular weights of 1,205, 1,718 Da respectively. The sequencing of peptides by MALDI-TOF MS/MS shows sequences QKALNEINQF and TKKTKLTEEEKNRL from α-S2 casein.

Keywords

Peptides Mass spectra Bioactive Enzymatic hydrolysis Antioxidant activity Bovine milk Casein Angiotensin converting enzyme inhibition 

Abbreviations

ACE

Angiotensin converting enzyme

ACEI

Angiotensin converting enzyme inhibition

DH

Degree of hydrolysis

DPPH 1

1-diphenyl-2-picrylhydrazyl

Gen/h

Generations per hour (growth rate)

IC50

Concentration of inhibitor at 50% inhibition

MALDI TOF

Matrix assisted laser desorption ionization time of flight

OPA

O-phthaldialdehyde

PEP

Prolyl endo peptidase

RP

Reverse phase

TFA

Trifluoroacetic acid

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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Department of Protein Chemistry and TechnologyCentral Food Technological Research Institute (A Constituent Laboratory of CSIR)MysoreIndia

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