Hydrolysis of different milk caseins by enzymatic extract from solanum dubium fresen seeds
2009
Fathelrahman, A.B.
Three milk types; bovine, ovine and caprine were used in this study to investigate the hydrolysis pattern of their caseins by a purified Solanum dubium Fresen seeds enzymatic extract using SDS-PAGE. The Solanum dubium Fresen seeds enzymatic extract used was checked for its purity by SDS-PAGE. The electrophoretogram of the enzyme showed one band with molecular mass of 66 kDa, the non appearance of any other bands ensures that the enzyme is pure; also shows that the enzyme is plant serine proteases because their molecular masses vary from 19 to 110 kDa. The proteolytic activity of the enzyme towards Na-caseinate previously prepared from the three milk types was studied by using. The resulting electrophoretograms showed that the bovine three main casein components a, B, and K-caseins, were sensitive to the action of Solanum dubium milk-clotting enzyme. B-casein was completely degraded during 3h incubation, while complete degradation of a-casein occurred after 6 h indicating its slow attack by the enzyme than B-casein. Bovine whole casein was hydrolyzed remaining one of the bands with no more hydrolysis up to 24 h; this band had a molecular mass of 16 kDa and assumed to be para- K -casein band. Bovine K-casein was completely degraded after 12 h of incubation another band appeared and its intensity increased with the time of incubation which is also assumed to be para- K -casein band. Ovine and caprine whole caseins showed similar hydrolysis pattern, for both a and B caseins showed progressive degradation but Caprine B-caseins a-caseins hydrolysis was much more rapid
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