Caseins and Casein Hydrolysates. 1. Lipoxygenase Inhibitory PropertiesClick to copy article linkArticle link copied!
Abstract
Whole casein from bovine origin, the different casein subtypes α, β, and κ, 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 β-casein were digested by proteases (trypsin, clostripain, and subtilisin). The β-casein tryptic digest and the tryptic and subtilisin digests of whole casein retained their inhibitory properties. The tryptic β-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 several lipoxygenase inhibitory peptides, corresponding mainly to the C-terminal moiety of β-casein, were identified.
Keywords: Soybean lipoxygenase 1; Lox-1 inhibitory β-casein peptides; FPLC; RP-HPLC; ESI-MS
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