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2008 | 58 | 4 |
Tytuł artykułu

Immunogenic potential of antigens isolated from trypsin pea protein hydrolysates

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
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.
Słowa kluczowe
EN
Wydawca
-
Rocznik
Tom
58
Numer
4
Opis fizyczny
p.491-496,fig.,ref.
Twórcy
  • Chair of Biochemistry, Faculty of Biology, Warmia and Mazury University in Olsztyn, Poland
autor
autor
Bibliografia
  • 1. Adler-Nissen J., Determination of the degree of hydrolysis of food protein hydrolyzates by trinitrobenzenesulfonic acid. J. Agr. Food Chem. 1979, 27, 1256–1260.
  • 2. AOAC. 1990. Official Methods of Analysis, 15th ed; Association of Official Analytical Chemists: Washington DC.
  • 3. Casey R., Pea legumins and vicilins. 2003, in: Idustrial Proteins in Perspective. Progress in Biotechnology (eds. W.Y Aalbersberg et al.). Elsevier Science: Amsterdam, The Netherlands, pp. 23, 55–62.
  • 4. Casey R., Domoney C., Pea globulins. 1999, in: Seed Proteins (eds. R.P Shewry, R. Casey). Kluwer Academic Publisher: Amsterdam, The Netherlands, pp. 171–208.
  • 5. Ena J.M., Van Beresteijn E.C.H., Robben J.P.M., Schmidt D.G., Protein antigenicity reduction by fungal proteinases and a pepsin/pancreatin combination. J. Food Sci., 1995, 60, 104–110.
  • 6. Engval E., Perlman P., Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry, 1971, 3, 871–876.
  • 7. Frączek R.J., Kostyra E., Kostyra H., Krawczuk S., Immunoreactive properties of pea protein extract and its trypsin hydrolysates. J. Anim. Feed Sci., 2007, 16, 472–484.
  • 8. Gendel S.M., Sequence database for assessing the potential allergenicity of proteins used in transgenic foods. Adv. Food Nutr. Res., 1998, 42, 63–91.
  • 9. Gruppen H., de Groot J., van Oort M.G., Identification and partial isolation of an antigenic protein Pisum sativum cv. Solara. 1993, in: Recent Advances of Research on Antinutritional Factors in Legumes Seeds. (eds. A.F.B. van der Poel et al.). Wageningen Press, The Netherlands, pp. 293–297.
  • 10. Guzmán-Partida A.M., Robles-Burgueño M.R., Ortega-Nieblas I., Vázquez-Moreno I., Purification and characterization of complex carbohydrate specific isolectins from wild legume seeds: Acacia constricta is (vinorama) highly homologous to Phaseolus vulgaris lectins.. Biochimie, 2004, 4–5, 335–342.
  • 11. Hajos G., Elias I., Halask A., Methionine enrichment of milk protein by enzymatic peptide modification. J. Food Sci., 1988, 53, 739–742.
  • 12. Hyun Soo Shin, Sang Bum Kim, Soo Cheol Kang, Muhammad Ajmal Khan, Hyeon Shup Kim, Hyun Jung Shin, Chi Hoon Chang, Production of low antigenic cheese whey protein hydrolysates using mixed proteolytic enzymes. J. Sci. Food Agric., 2007, 87, 2055–2060.
  • 13. Laemmli U.K., Cleavage of structural proteins during the assembly of the head bacteriophage T 4. Nature, 1970, 227, 680–685.
  • 14. McLeester R.C., Hall T.C., Sun S.M., Bliss F.A., Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba. Phytochemistry, 1973, 2, 85–93.
  • 15. Newbigin E.J., Do Lumen B.O., Chendler P.M., Gould A., Pea convicilin: structure and primary sequence of the protein and expression of a gene in the seeds of transgenic tobacco. Planta, 1990, 180, 461–470.
  • 16. O’Kane F.E., Happe R.P., Vereijken J.M., Gruppen H., Van Boekel MAJS., Characterisation of pea vicilin. 2. Consequences of compositional heterogeneity on heat-induced gelation behavior. J. Agr. Food Chem., 2004, 52, 143–154.
  • 17. Sanchez-Monge R., Lopez-Torrejon G., Pascual CY., Varela J., Martin-Esteban M., Salcedo G., Vicilin and convicilin are potential major allergens from pea. Clin. Exp. Allergy., 2004, 34, 1747–1753.
  • 18. Sheldon P.S., Keen J.N., Bowles D.J., Post-translational peptide bond formation during concavalin A processing in vitro. Biochem. J., 1996, 320, 865–870.
  • 19. Tzitzikas E.N., Vincken J.P., De Groot J., Gruppen H., Visser R G.F., Genetic variation in pea globulin composition. J. Agr. Food Chem., 2006, 54, 425–433.
  • 20. Wang T.L., Domoney C., Hedley L., Casey R, Grusak M.A., Can we improve the nutritional quality of legume seeds? Plant Physiol., 2003, 131, 886–891.
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