Immunoreactive properties of pea protein extract and its trypsin hydrolysates
R. J. Frączek 1,   E. Kostyra 1,   H. Kostyra 2  
,   S. Krawczuk 1
 
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1
Faculty of Biology, Chair of Biochemistry,Warmia and Mazury University, Oczapowskiego 1A, 10-957 Olsztyn, Poland
2
Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland
CORRESPONDING AUTHOR
H. Kostyra   

Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland
Publication date: 2007-09-06
 
J. Anim. Feed Sci. 2007;16(3):472–484
 
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ABSTRACT
The study was undertaken to examine the immunogenic potential of pea protein of Polish variety Rodan and its trypsin hydrolysates differing in degree of hydrolysis. The physicochemical characteristic of pea protein extract and its hydrolysates, DH 2.0 and 5.0, were determined by 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 confirmed that protein extract is a stronger immunogen than hydrolysates, while hydrolysate DH 2.0 was a stronger immunogen than DH 5.0. The dominant antigen isolated from pea protein extract and both trypsin hydrolysates had a molecular weight of about 20 kDa and was in the glycoprotein fraction. The N-terminal sequence of this antigen was determined to be: Thr-Glu-Thr-Thr-Ser-Phe-Leu-Ile-Thr-Lys-.
ISSN:1230-1388