[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

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

Srinivas, S. and Prakash, V. (2010) Bioactive Peptides from Bovine Milk a-Casein: Isolation, Characterization and Multifunctional properties. International Journal of Peptide Research and Therapeutics , 16:. pp. 7-15.

[img] PDF
Int_J_Pept_Res_Ther_(2010)_16_7–15.pdf
Restricted to Registered users only

Download (447kB)

Abstract

a-Casein group of proteins makes up to 65% of the total casein and consists of aS1- casein, aS2- 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 a-S2 casein.

Item Type: Article
Uncontrolled Keywords: Peptides � Mass spectra � Bioactive � Enzymatic hydrolysis � Antioxidant activity � Bovine milk � Casein � Angiotensin converting enzyme inhibition
Subjects: 600 Technology > 08 Food technology > 27 Dairy products
500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 25 Peptide Chemistry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 30 Nov 2010 07:04
Last Modified: 28 Dec 2011 10:20
URI: http://ir.cftri.com/id/eprint/9812

Actions (login required)

View Item View Item