Effect of proteolytic modification and methionine enrichment on the nutritional value of soya albumins for rats
1996
Hajós, György | Gelencser, E. | Grant, G. | Bardocz, S. | Sakhri, M. | Duguid, T.J. | Newman, A.M. | Pusztai, A.
Proteolytic modification, particularly when combined with methionine enrichment, significantly reduced the lectin content and modified the trypsin inhibitor activity of a soya albumin preparation. During both peptic hydrolysis and enzymatic peptide modification, the amount of soya bean agglutinin was reduced. This reduction was verified by the decrease in the intensity of protein staining and immunoblots of the peptic hydrolysate and of the product produced by enzymatic peptide modification, and confirmed by haemagglutination activity measurements and ELISA technique. The junctional activity of Kunitz trypsin inhibitor was also partially abolished whereas that of the Bowman-Birk inhibitor was not significantly altered by the enzymatic modifications. In line with the reduction in some of the antinutrients, the nutritional performance of rats fed a diet containing this enzymatically modified product was significantly improved in comparison with that of the control animals fed the original soya albumin but was poorer than the lactalbumin fed controls. Enzymatic peptide modification of soya albumin fractions by transpeptidation and covalent methionine enrichment is suitable to improve their nutritional value party by compensating for their methionine deficiency and party by modifying the structure of the soya antinutrients. Changes in the structure by proteolytic hydrolysis and synthesis of peptide chains can lead to alteration in protein conformation, resulting in modified biological activity and increased nutritional value.
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