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 ingredients 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