Preparation of Antioxidant Enzymatic Hydrolysates from α-Lactalbumin and β-Lactoglobulin. Identification of Active Peptides by HPLC-MS/MS
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- 14 January 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 53 (3), 588-593
- https://doi.org/10.1021/jf048626m
Abstract
We have investigated the antioxidant activity of hydrolysates from whey proteins bovine alpha-lactalbumin (alpha-La) and beta-lactoglobulin A (beta-Lg A) by commercial proteases (pepsin, trypsin, chymotrypsin, thermolysin, and Corolase PP). Corolase PP was the most appropriate enzyme to obtain antioxidant hydrolysates from alpha-La and beta-Lg A (ORAC-FL values of 2.315 and 2.151 micromol of Trolox equivalent/mg of protein, respectively). A total of 42 peptide fragments were identified by HPLC-MS/MS in the beta-Lg A hydrolysate by Corolase PP. One of the sequences (Trp-Tyr-Ser-Leu-Ala-Met-Ala-Ala-Ser-Asp-Ile) possessed radical scavenging (ORAC-FL value of 2.621 micromol of Trolox equivalent/micromol of peptide) higher than that of butylated hydroxyanisole (BHA). Our results suggest that whey protein hydrolysates could be suitable as natural ingredients in enhancing antioxidant properties of functional foods and in preventing oxidation reaction in food processing.Keywords
This publication has 15 references indexed in Scilit:
- Angiotensin Converting Enzyme Inhibitory Activity in Commercial Fermented Products. Formation of Peptides under Simulated Gastrointestinal DigestionJournal of Agricultural and Food Chemistry, 2004
- Extending Applicability of the Oxygen Radical Absorbance Capacity (ORAC−Fluorescein) AssayJournal of Agricultural and Food Chemistry, 2003
- Preparation of ovine and caprine β-lactoglobulin hydrolysates with ACE-inhibitory activity. Identification of active peptides from caprine β-lactoglobulin hydrolysed with thermolysinInternational Dairy Journal, 2002
- ConclusionsMolecular Aspects of Medicine, 2002
- Antigenic response of whey proteins and genetic variants of β-lactoglobulin — the effect of proteolysis and processingInternational Dairy Journal, 2000
- Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin: In situ enzymatic hydrolysis on an ion-exchange membraneJournal of Chromatography A, 1999
- Antioxidative Activity of Soluble Elastin PeptidesJournal of Agricultural and Food Chemistry, 1998
- The characterization of antioxidantsFood and Chemical Toxicology, 1995
- Antioxidative Activity of Peptides Prepared by Enzymatic Hydrolysis of Egg-white Albumin.Journal of the agricultural chemical society of Japan, 1991
- Letter to the editorsJournal of Mass Spectrometry, 1984