Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 49, Issue 1, Pages 287-294Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf000392t
Keywords
soybean lipoxygenase 1; Lox-1 inhibitory beta-casein peptides; FPLC; RP-HPLC; ESI-MS
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available