Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulln. Identification of active peptides by HPLC-MS/MS

Abstract:

We have investigated the antioxidant activity of hydrolysates from whey proteins bovine α-lactalbumin (α-La) and β-lactoglobulin A (β-Lg A) by commercial proteases (pepsin, trypsin, chymotrypsin, thermolysin, and Corolase PP). Corolase PP was the most appropriate enzyme to obtain antioxidant hydrolysates from α-La and β-Lg A (ORAC-FL values of 2.315 and 2.151 μmol of Trolox equivalent/ mg of protein, respectively). A total of 42 peptide fragments were identified by HPLC-MS/MS in the β-Lg A hydrolysate by Corolase PP. One of the sequences (Trp-Tyr-Ser-Leu-Ala-Met-Ala- Ala-Ser-Asp-IIe) possessed radical scavenging (ORAC-FL value of 2.621 μmol of Trolox equivalent/umol of peptide) higher than that of butylated hydroxyanisole (BHA). Our results suggest that whey protein hydrolysates could be suitable as natural ingbkp_redients in enhancing antioxidant properties of functional foods and in preventing oxidation reaction in food processing.

Año de publicación:

2005

Keywords:

• Peptides
• α-Lactalbumin
• β-lactoglobulln
• Mass spectrometry
• Radical scavenging activity

Fuente:

scopus