Toxicological studies on plant proteins: a review

作者: Wenbiao Wu , Rong Sun

DOI: 10.1002/JAT.1780

关键词:

摘要: Nowadays, toxicological studies are contributing to human health more than ever. Reports on the of plant proteins, which continuously growing in number literature, have been reviewed. Two important aspects discussed: dietary safety evaluation, including toxicity tests and maximum daily intake allowance, appropriate proportion our diets proteins from traditional foods new sources not traditionally employed as foods. Water hyacinth leaf sweet lupin canola shown be toxic, although they food proteins. These findings very for exploiting valuable protein that suitable or animal consumption applicable industry. Acutely toxic lectins, ribosome-inactivating inhibitors proteolytic enzymes glycohydro-lases, isolated materials identified. Their toxicities molecular characteristics described. The depends upon their specific native structures. Once denatured by treatment, such heating, can reduced even eliminated. indicate raw contain this kind edible. However, after proper processing, may consumption. Although type 2 reported different authors vary, dosages still trace amounts.

参考文章(99)
W. Montfort, J.E. Villafranca, A.F. Monzingo, S.R. Ernst, B. Katzin, E. Rutenber, N.H. Xuong, R. Hamlin, J.D. Robertus, The Three-dimensional Structure of Ricin at 2.8 A* Journal of Biological Chemistry. ,vol. 262, pp. 5398- 5403 ,(1987) , 10.1016/S0021-9258(18)61201-3
Ramon S Hall, Stuart K Johnson, Sarah J Thomas, Australian sweet lupin flour addition reduces the glycaemic index of a white bread breakfast without affecting palatability in healthy human volunteers. Asia Pacific Journal of Clinical Nutrition. ,vol. 14, pp. 91- 97 ,(2005)
Ana Paula Ulian Araújo, Priscila Vasques Castilho, Leandro Seiji Goto, Ribosome-Inactivating Proteins from Abrus pulchellus Springer, Berlin, Heidelberg. pp. 133- 147 ,(2010) , 10.1007/978-3-642-12176-0_7
W. Min, A.J. Dunn, D.H. Jones, Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage. The EMBO Journal. ,vol. 11, pp. 1303- 1307 ,(1992) , 10.1002/J.1460-2075.1992.TB05174.X
L Barbieri, M Zamboni, L Montanaro, S Sperti, F Stirpe, Purification and properties of different forms of modeccin, the toxin of Adenia digitata. Separation of subunits with inhibitory and lectin activity. Biochemical Journal. ,vol. 185, pp. 203- 210 ,(1980) , 10.1042/BJ1850203
K Sandvig, S Olsnes, A Pihl, Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells. Journal of Biological Chemistry. ,vol. 251, pp. 3977- 3984 ,(1976) , 10.1016/S0021-9258(17)33344-6
Priscila V. Castilho, Leandro S. Goto, Lynne M. Roberts, Ana Paula U. Araújo, Isolation and characterization of four type 2 ribosome inactivating pulchellin isoforms from Abrus pulchellus seeds. FEBS Journal. ,vol. 275, pp. 948- 959 ,(2008) , 10.1111/J.1742-4658.2008.06258.X
Thomas B. Osborne, Lafayette B. Mendel, Edna L. Ferry, Alfred J. Wakeman, THE USE OF SOY BEAN AS FOOD Journal of Biological Chemistry. ,vol. 32, pp. 369- 387 ,(1917) , 10.1016/S0021-9258(18)86623-6
J. Michael Lord, Lynne M. Roberts, Jon D. Robertus, Ricin: structure, mode of action, and some current applications. The FASEB Journal. ,vol. 8, pp. 201- 208 ,(1994) , 10.1096/FASEBJ.8.2.8119491
André LC Silva, Leandro S Goto, Anemari R Dinarte, Daiane Hansen, Renato A Moreira, Leila M Beltramini, Ana PU Araújo, None, Pulchellin, a highly toxic type 2 ribosome-inactivating protein from Abrus pulchellus. Cloning heterologous expression of A-chain and structural studies. FEBS Journal. ,vol. 272, pp. 1201- 1210 ,(2005) , 10.1111/J.1742-4658.2005.04545.X