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Abstract
An emulsion was prepared by homogenizing soybean oil with an αs1-casein solution. The αs1-Blcasein adsorbed to the oil/water interface in the emulsion was digested with trypsin and then analyzed by reversed-phase high-performance liquid chromatography. Two peaks, T-1 and T-2E, due to the same fragment (194Thr-Thr-Met-Pro-Leu-Trp) were found. Amino acid analysis showed that the 196Met of T-l had been oxidized to methionine sulfoxide, and the NMR spectrum indicated that the 196Met-Pro bond of T-1 had been subjected to cis-trans isomerization. The isomerization of the same peptide bond was also observed when this peptide fragment was oxidized by chloramine-T in solution, suggesting that cis-trans isomerization of 197Pro was induced by 196Met oxidation.
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