G. Hajos et al., EFFECT OF PROTEOLYTIC MODIFICATION AND METHIONINE ENRICHMENT ON THE NUTRITIONAL-VALUE OF SOYA ALBUMINS FOR RATS, Journal of nutritional biochemistry, 7(9), 1996, pp. 481-487
Proteolytic modification, particularly when combined with methionine e
nrichment, significantly reduced the lectin content and modified the t
rypsin inhibitor activity of a soya albumin preparation. During both p
eptic hydrolysis and enzymatic peptide modification, the amount of soy
a bean agglutinin was reduced. This reduction was verified by the decr
ease in the intensity of protein staining and immunoblots of the pepti
c hydrolysate and of the product produced by enzymatic peptide modific
ation, and confirmed by haemagglutination activity measurements and EL
ISA technique. The functional activity of Kunitz trypsin inhibitor was
also partially abolished whereas that of the Bowman-Birk inhibitor wa
s not significantly altered by the enzymatic modifications. In line wi
th the reduction in some of the antinutrients, the nutritional perform
ance of rats fed a diet containing this enzymatically modified product
was significantly improved in comparison with that of the control ani
mals fed the original soya albumin but was poorer than the lactalbumin
-fed controls. Enzymatic peptide modification of soya albumin fraction
s by transpeptidation and covalent methionine enrichment is suitable t
o improve their nutritional value partly by compensating for their met
hionine deficiency and partly by modifying the structure of the soya a
ntinutrients. Changes in the structure by proteolytic hydrolysis and s
ynthesis of peptide chains can lead to alteration in protein conformat
ion resulting in modified biological activity and increased nutritiona
l value.