Caseins and Casein Hydrolysates. 1. Lipoxygenase Inhibitory Properties
作者:Sandrine G. Rival、Silvia Fornaroli、Carmen G. Boeriu、Harry J. Wichers
DOI:10.1021/jf000392t
日期:2001.1.1
Whole casein from bovine origin, the different casein subtypes alpha, beta, and kappa, and the related dephosphorylated proteins were assayed as modulators of soybean lipoxygenase 1 activity and were found to inhibit it. To define the lipoxygenase inhibitory domain, whole casein and beta -casein were digested by proteases (trypsin, clostripain, and subtilisin). The beta -casein tryptic digest and the tryptic and subtilisin digests of whole casein retained their inhibitory properties. The tryptic beta -casein digest was the most potent inhibitor of lipoxygenase activity and was further fractionated by FPLC or HPLC. The collected peptides inhibited the lipoxygenase-catalyzed reaction to different extents. The active fractions were analyzed by ESI-MS, and the sequences of sever al lipoxygenase inhibitory peptides, corresponding mainly to the C-terminal moiety of beta -casein, were identified.