Casein hydrolysis by Bifidobacterium longum KACC91563 and antioxidant activities of peptides derived therefrom
2013
Chang, O.K. | Seol, K.-H. | Jeong, S.-G. | Oh, M.-H. | Park, B.-Y. | Perrin, C. | Ham, J.-S.
Milk protein is a well-known precursor protein for the generation of bioactive peptides using lactic acid bacteria. This study investigated the antioxidant activity of bovine casein hydrolysate after fermentation with Bifidobacterium longum KACC91563 using the 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) assay and total phenolic content (TPC). The antioxidant activities of the 24-h and 48-h hydrolysates were higher than that of the 4-h hydrolysate (2,045.5 and 1,629.3μM gallic acid equivalents, respectively, vs. 40.3μM) in the ABTS assay. In contrast, TPC values showed activities of 43.2 and 52.4μM gallic acid equivalents for the 4-h and 24-h hydrolysates, respectively. Three fractions (≥10kDa, ≥3 but <10kDa, and <3kDa) were separated from the 24-h hydrolysate by ultrafiltration. Among these fractions, the <3kDa fraction exhibited the highest antioxidant activity (936.7μM) compared with the other fractions (42.1 and 34.2μM for >10kDa and 3–10kDa fractions, respectively). Through liquid chromatography-electrospray ionization-tandem mass spectrometry analysis, 2 peptides, VLSLSQSKVLPVPQK and VLSLSQSKVLPVPQKAVPYPQRDMPIQA, containing the fragment VLPVPQ that has antioxidant properties, were identified in the <3kDa fraction after 24h of hydrolysis. The present study demonstrates the possibility of antioxidant peptide production from bovine casein using Bifidobacterium longum.
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