Casein hydrolysis by Bifidobacterium longum KACC91563 and antioxidant activities of peptides derived therefrom.

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 µM gallic acid equivalents, respectively, vs. 40.3 µM) in the ABTS assay. In contrast, TPC values showed activities of 43.2 and 52.4 µM 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 µM) compared with the other fractions (42.1 and 34.2 µM for >10 kDa and 3-10 kDa 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.

Determination of molecular weights of caprine milk proteins by matrix-assisted laser desorption/ionization mass spectrometry.

Molecular weights (MW) of major proteins in milk of 3 Korean dairy goat breeds were determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, after treatment of milk samples with the reduction buffer used in capillary electrophoresis. The MW of caprine milk proteins were compared with those of Holstein milk counterparts using commercial bovine milk protein standards. The MW of α-lactalbumin, ß-lactoglobulin, and α- and ß-casein standards were 14,197±3.4, 18,326±26.3, 23,591±13.0, and 23,967±12.8 m/z, respectively, whereas those of Holstein milk treated with the reduction buffer were 14,199±8.3, 18,397±25.9, 23,614±64.8, and 23,984±75.6 m/z, respectively. The respective MW of α-lactalbumin in Saanen, Toggenberg, and Alpine milk were 14,194±27.2, 14,266±105.9, and 14,241±13.2 m/z, which were not different from those of the bovine milk. The respective MW of ß- lactoglobulin in corresponding caprine milk were 18,840±31.5, 18,856±26.3, and 18,857±21.3 m/z, which were higher than those in the bovine milk. The MW of ß-casein in corresponding caprine milk were 23,860±27.2, 23,886±12.3, and 23,901±8.4 m/z, which were lower than those in the bovine milk. The results indicated that matrix-assisted laser desorption/ionization time-of-flight mass spectrometry could be used for rapid determination of MW of Korean caprine milk proteins without protein separation steps.

Effects of temperature conditioning on postmortem changes in physico-chemical properties in Korean native cattle (Hanwoo).

The objective of this study was to examine the changes in physico-chemical properties that occur after adjusting postmortem chilling temperatures in Hanwoo beef. The right sides of beef carcasses were chilled for 4h at 2°C, 4h at 12°C and 16h at 2°C. The left sides were used as controls, chilled for 24h at 2°C. It took 8h for the control carcasses to cool down to <10°C and 10h 20min for the treatment. Adjusting the chilling temperature could be effective in lowering the postmortem pH and glycogen content. Treatment muscles at least 8h postmortem had longer sarcomeres than the control (P<0.05). The shear force in treatment carcasses at day 1 was similar to that of the control at day 6. Alternate chilling temperature had no detrimental effect on drip, cooking, total loss or color. Total numbers of aerobic plate counts were not significantly different between the control and treatment.