IMMUNOGENIC POTENTIAL OF ANTIGENS ISOLATED FROM TRYPSIN PEA PROTEIN HYDROLYSATES
 
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Pol. J. Food Nutr. Sci. 2008;58(4):491–496
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ABSTRACT
The study was undertaken to examine the immunogenic potential of pea protein of Polish cultivar Maraton and its trypsin hydrolysates differing in a degree of hydrolysis. The physicochemical characteristics of a pea protein extract and its hydrolysates, DH 2.0 and 5.0, was conducted by means of SDS-PAGE electrophoresis, chromatofocusing, affinity chromatography, and sequential analysis. The immunogenic properties of pea protein and its trypsin hydrolysates, DH 2.0 and 5.0, were investigated by direct and competitive ELISA methods. The results confirm that the protein extract is a stronger immunogene than the hydrolysates, while hydrolysate with DH 2.0 was a stronger immunogene than that with DH 5.0. The dominant antigen isolated from the pea protein extract and both trypsin hydrolysates had a molecular weight of about 20 kDa and was in glycoprotein fraction. The N-terminal sequence of this antigen was determined to be: Thr-Glu-Thr-Thr-Ser-Phe-Leu-Ile-Thr-Lys. Its precursor is probably pea lectin.
ISSN:1230-0322