Bovine serum albumin hydrolyzates (BSA-H) were prepared by the hydrolysis of BSA with pepsin, trypsin, chymotrypsin, or the combinations of these enzymes. In the presence of BSA-H, linoleic acid was oxidized in an ethanol-phosphate buffer (pH 7.0) system at 60°C in the dark, and the extent of lipid oxidation was measured by the ferric thiocyanate method.
The antioxidative activity of BSA-H depended on the degree of hydrolysis but not on the particular enzyme or enzyme combination used. The antioxidative activity of BSA-H, however, was not as strong as ordinary antioxidants such as butylhydroxyanisol, butylhydroxytoluene, α-tocopherol or sodium ascorbate.
BSA-H used with each antioxidant considerably enhanced in each case antioxidative activity, thus indicating BSA-H to be a useful synergists.
BSA-H prepared with pepsin was separated into several peaks by Sephadex G-25 chromatography, and a particular group, comprised of relatively high molecular weight polypeptides, showed strong synergistic effect with each antioxidant.
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