Effect of enzymatic modification on the biological activity and nutritive value of cow and buffalo casein

Hussein, S. and Gelencsér, É. and Polgár, M. and Hajós, György (2000) Effect of enzymatic modification on the biological activity and nutritive value of cow and buffalo casein. Acta Alimentaria, 29 (3). pp. 273-288. ISSN 0139-3006

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Abstract

Buffalo and cow milk caseins were submitted to hydrolysis either with á -chymotrypsin or with pepsin. Enzymatic peptide modification (EPM) was carried out by using L-methionine ethyl ester in the reaction mixture. As catalyst, á -chymotrypsin or pepsin was used. The incorporation of methionine in to the peptide chains in the presence of á -chymotrypsin showed an optimum value at 0.14 g Met added to the reaction mixture/1 g hydrolysate in both cases. In the case of pepsin used as catalyst, the optimal Met-enrichment was at 0.14 g Met added to the reaction mixture/1 g buffalo casein hydrolysate and at 0.34 g Met/1 g cow casein hydrolysate. The covalent nature of the amino acid incorporation was confirmed by SDS - polyacryl amide gel electrophoresis in the presence of urea. Electrophoretic patterns of the products indicate that transpeptidation plays an essential role in the EPM reaction. Antigenic character of the EPM- products was investigated in vitro by competitive indirect ELISA. Enzymatic peptide modification with methionine enrichment seems to be an efficient method for the reduction of the antigenic/potential allergenic character and for the improvement of the nutritive value of buffalo and cow milk caseins.

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