Journal
JOURNAL OF DAIRY SCIENCE
Volume 96, Issue 9, Pages 5544-5555Publisher
ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2013-6687
Keywords
Bifidobacterium longum; antioxidant; bioactive peptide; casein hydrolysis
Funding
- National Institute of Animal Science (NIAS) research project of Rural Development Administration of Korea (RDA) [PJ0085852013]
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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 1,629.3 mu M gallic acid equivalents, respectively, vs. 40.3 mu M) in the ABTS assay. In contrast, TPC values showed activities of 43.2 and 52.4 mu M gallic acid equivalents for the 4-h and 24-h hydrolysates, respectively. Three fractions (>= 10 kDa, >= 3 but <10 kDa, and <3 kDa) were separated from the 24-h hydrolysate by ultrafiltration. Among these fractions, the <3 kDa fraction exhibited the highest antioxidant activity (936.7 mu M) compared with the other fractions (42.1 and 34.2 mu M for >10 kDa and 3-10 kDa fractions, respectively). Through liquid chromatography-electrospray ionization-tandem mass spectrometry analysis, 2 peptides, VLSLSQSKVLPVPQK and VLSLSQSKVLPVPQKA-VPYPQRDMPIQA, containing the fragment VLPVPQ that has antioxidant properties, were identified in the <3 kDa fraction after 24 h of hydrolysis. The present study demonstrates the possibility of antioxidant peptide production from bovine casein using Bifidobacterium longum.
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