Proteoliza limitată cu papaină a extractelor proteinelor nepurificate din seminţele de arahide şi soia duce la scindarea regiunii C-terminale a domeniilor N-terminale ale globulinelor 11S, precum şi a regiunii N-terminale a globulinei 7S din arahide. În aceste domenii au fost identificaţi epitopii IgE, care determină în mare măsură alergenicitatea globuline­lor 11S şi 7S din arahide şi soia. Rezultatele obţinute indică posibilitatea fundamentală de reducere a alergenicităţii proteinelor din arahide şi soia atunci când se utilizează ca substraturi nu doar preparatele purificate de globuline, aşa cum s-a stabilit anterior, dar şi extractele de proteine totale din seminţe.




Limited papain proteolysis of unpurified protein extracts from peanut and soybean seeds leads to cleavage off of the C-terminal region of the N-terminal domains of 11S globulins, as well as the N-terminal region of peanut 7S globulin. In these regions, IgE epitopes have been identified, largely determining the allergenicity of 11S and 7S peanut and soybean globulins. The results indicate the fundamental possibility of reducing the allergenicity of peanut and soybean proteins when using not only purified globulin preparations as substrates, as established earlier, but also total protein extracts of seeds.


seed storage globulins, allergens, IgE epitopes, peanut, soybean.

Full Text:



DUNWELL, J.M. Structure, function, and evolution of vicilin and legumin seed storage proteins. In: A. Steinbüchel, Y. Doi, eds. Biotechnology of biopolymers - from synthesis to patents. Wiley-VCH Verlag GmbH & Co. KgaA: Weinheim, 2005, p.967-997.

IVANCIUK, O., SCHEIN, C.H., BRAUN, W. SDAP: database and computational tools for allergenic proteins. In: Nucleic Acid Research, 2003, vol.31, p.359-362 (doi: 10.1093/nar/gkg010).

PELE, M. Peanut allergens. In: Romanian Biothechnological Letters, 2010, vol.15, p.5204-5212.

CHERDIVARĂ, A.M. Limited proteolysis as a means to reduce the allergenicity of seed storage globulins (review). In: Agricultural Biology, 2018, v.53, p.475-484 (doi: 10.15389/agrobiology.2018.3.475eng).

SHUTOV, A.D., WILSON, K.A. Seed storage globulins: their descent from bacterial ancestors and mechanisms of degradation. In: S.D. Milford, ed. Globulins: Biochemistry, Production and Role in Immunity. Nova Science Publishers: New York, 2014, p.71-104.

RABJOHN, P., HELM, E.M., STANLEY, J.S. et al. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. In: Journal of Clinical Investigation, 1999, vol.103, p.535-542 (doi: 10.1172/JCI5349).

SHIN, D.S., COMPADRE, C.M., MALEKI, S.J. et al. Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein. In: Journal of Bioljgical Chemistry, 1998, v.273, p. 13753-13759 (doi: 10.1074/jbc.273.22.13753).

CHERDIVARĂ, A., RUDAKOVA, A., RUDAKOV, S., ŞUTOV, A. Alergenul Ara h3, globulina de rezervă din seminţele de arahide. 2. Proteoliza limitată cu tripsină. În: Studia Universitatis Moldaviae, seria Ştiinţe reale şi ale naturii, 2017, 1(101), p.41-45.

CHERDIVARĂ, A., RUDAKOVA, A., RUDAKOV, S., SHUTOV, A. Proteoliza limitată a alergenului Ara h1, globulina de rezervă 7S din seminţele de arahide. În: Studia Universitatis Moldaviae, seria Ştiinţe reale şi ale naturii, 2016, 6(96), p.10-15.

BEARDSLEE, T.A., ZEECE, M.G., SARATH, G., MARKWELL, J. P. Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. In: International Archives of Allergy and Immunology, 2000, vol.123, p.299-307.

SHUTOV, A., RUDAKOVA, A., RUDAKOV, S., KAKHOVSKAYA, I. et al. Limited proteolysis regulates massive degradation of glycinin, storage 11S globulin from soybean seeds: an in vitro model. In: Journal of Plant Physiology, 2012, vol.169, p.1227-1233 (doi: 10.1016/j.jplph.2012.06.004).

CHERDIVARĂ, A., RUDAKOVA, A., RUDAKOV, S., ŞUTOV, A. Alergenul Ara h3, globulina de rezervă din seminţele de arahide. 1. Proteoliza limitată cu papaină. În: Studia Universitatis Moldaviae, seria Ştiinţe reale şi ale naturii, 2017, 1(101), p.37-40.

LAEMMLI, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. In: Nature, 1970, vol.227, p.680-685.

SCHECHTER, I., BERGER, A. On the size of the active site in proteases. I. Papain. In: Biochemical and Biophysical Research Communications, 1967, vol.27, p.157-162.

ARNOLD, K., BORDOLI, L., KOPP, J., SCHWEDE, T. The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. In: Bioinformatics 2006, vol.22, p.195-201.

RUPLEY, J.A. Susceptibility to attack by proteolytic enzymes. In: Methods Enzymology, 1967, vol.11, p.905-917.

SHUTOV, A.D., PINEDA, J., SENYUK, V.I. et al. Action of trypsin on soybean glycinin. Mixed-type proteolysis and its kinetics; molecular mass of glycinin-T. In: European Journal of Biochemistry, 1991, vol.199, p.539-543.

VAINTRAUB, I.A. Kinetics of co-operative proteolysis. In: Nahrung, 1998, vol.42, p.59-60.

SHUTOV, A.D., RUDAKOVA, A.S., RUDAKOV, S.V. et al. Degradation of β-conglycinin β-homotrimer by papain: independent occurrence of limited and extensive proteolyses, In: Bioscience, Biotechnology and Biochemistry, 2013, vol.77, p.2082-2086.

NIELSEN, N.C, NAM, Y-W. (1999) Soybean globulins. In: P.R. Shewry, R. Casey, eds. Seed proteins. The Netherlands, Kluwer Academic Publishers: Dordrecht, p.285-313.

SHUTOV, A.D., KAKHOVSKAYA, I.A., BASTRYGINA, A.S. et al. Limited proteolysis of β-conglycinin and glycinin, the 7S and 11S storage globulins from soybean (Glycine max (L.) Merr.): structural and evolutionary implications, In: European Journal of Biochemistry, 1996, vol.241, p.221-228.


  • There are currently no refbacks.