Effects of ${\alpha}$-Chymotrypsin Modification on the Functional Properties of Soy Protein Isolates

  • Ahn Tae-Hyun (National Institute of Crop Science, RDA) ;
  • Lee Sook-Young (Department of Food and Nutrition, Chung-Ang University)
  • Published : 2006.06.01

Abstract

Effects of ${\alpha}$-chymotrypsin modification on degree of hydrolysis (DH), solubility, emulsifying capacity and thermal aggregation of laboratory-purified soy protein isolate (SPI) using a lipoxygenase-defected soybean (Jinpum-kong) and commercial soy protein isolate (Supro 500E) were compared. SPIs were hydrolyzed by ${\alpha}$-chymotrypsin at pH 7.8 and $37^{\circ}C$ for 30 min. DHs of Supro 500E and Jinpum-kong SPI were increased by ${\alpha}$-chymotrypsin modification, and DH of Supro 500E was higher than that of Jinpum-kong SPI. DH of ${\alpha}$-chymotrypsin treated Jinpum-kong SPI was similar with untreated Supro 500E and DH of treated Supro 500E was the highest. Solubility, emulsifying capacity and thermal aggregation of SPIs were increased by ${\alpha}$-chymotrypsin modification, and these changes were highly related to changes in DH. Functional properties of Supro 500E were higher than Jinpum-kong SPI in both of untreated and ${\alpha}$-chymotrypsin treated SPIs.

Keywords

References

  1. Anon, M. C., D. A. Sorgentini, and J. R. Wagner. 2001. Relation­ship between different hydration properties of commercial and laboratory soybean isolates. J. Agric. Food Chem. 49 : 4852-­4858 https://doi.org/10.1021/jf010384s
  2. Aoki, H., O. Taneyama, and M. Inami. 1980. EmulsifYing proper­ties of soy protein: characteristics of 7S and lIS proteins. J. Food Sci. 45 : 534-538 https://doi.org/10.1111/j.1365-2621.1980.tb04095.x
  3. Arrese, E. L., D. A. Sorgentini, J. R. Wagner, and M. C. Anon. 1991. Electrophoretic, solubility and functional properties of commercial soy protein isolates. J. Agric. Food Chem. 39 : 1029-1032 https://doi.org/10.1021/jf00006a004
  4. Association of Official Analytical Chemists (AOAC). 1975. Offi­cial Methods of Analysis. 12th ed. Association of Official Ana­lytical Chemists. Washington DC. p. 927
  5. Bollag, D. M. and S. J. Edelstein. 1991. Gel electrophoresis under denaturing conditions: In Protein methods. Wiley-Liss, Inc. pp. 95-127
  6. Brooks, J. R. and C. V. Morr. 1985. Current aspects of soy protein fractionation and nomenclature. J. Amer. Oil Chem. Soc. 62 : 1347-1354 https://doi.org/10.1007/BF02545956
  7. Campbell, N. F., F. F. Shih, J. S. Hamada, and W. E. Marshall. 1996. Effect of limited proteolysis on the enzymatic phospho­rylation of soy protein. J. Agric. Food Chem. 44: 759-762 https://doi.org/10.1021/jf950390m
  8. Chobert, J. M., C. Bertrand-Harb, and M. G. Nicolas. 1988. Solu­bility and emulsifYing properties of caseins whey protein mod­ified enzymatically by trypsin. J. Agric. Food Chem. 36 : 883-­892 https://doi.org/10.1021/jf00083a002
  9. Garcia Chacon, E. J., L. D. Satterlee, and M. A. Hanna. 1990. Heat induced gels from partially hydrolyzed soy protein isolate. J. Food Biochem. 14: 15-29 https://doi.org/10.1111/j.1745-4514.1990.tb00818.x
  10. German, B., S. Damodaran, and J. E. Kinsella. 1982. Thermal dis­sociation and association behavior of soy proteins. J. Agric. Food Chem. 30 : 807-811 https://doi.org/10.1021/jf00113a002
  11. Khatib, K. A., T. J. Herald, F. M. Aramouni, F. MacRitchie, and W. T. Schapaugh. 2002. Characterization and functional properties of soy ${\beta}$-conglycinin and glycinin of selected genotypes. J. Food Sci. 67: 2923-2929 https://doi.org/10.1111/j.1365-2621.2002.tb08839.x
  12. Kim(Lee), S. Y., P. S. W. Park, and K. C. Rhee. 1990. Functional properties of proteolytic enzyme modified soy protein isolate. J. Agric. Food Chem. 38 : 651-656 https://doi.org/10.1021/jf00093a014
  13. Kim(Lee), S. Y., P. S. W. Park, and K. C. Rhee. 1992. Textural properties of cheese analogs containing proteolytic enzyme­modified soy protein isolates. J. Amer. Oil Chem. Soc. 69 : 755-759 https://doi.org/10.1007/BF02635911
  14. Kim, Y. H. and S. D. Kim. 1994. Processing characteristics of soy­bean genotypes lacking lipoxygenase. Korean J. Crop Sci. 39 : 171-174
  15. Kinsella, J. E. 1979. Functional properties of soy proteins. J. Amer. Oil Chem. Soc. 56 : 242-258 https://doi.org/10.1007/BF02671468
  16. Kinsella, J. E., S. Damodaran, and B. German. 1985. Physico­chemical and functional properties of oilseed proteins with emphasis on soy protein. New Food Proteins 5: 107-178
  17. Kitamura, K. 1993. Breeding trials for improving the food process­ing quality of soybean. Trends Food Sci. Techol. 4: 64-67 https://doi.org/10.1016/0924-2244(93)90186-E
  18. Kobayashi, A., Y. Tsuda, N. Hirata, K. Kubota, and K. Kitamura. 1995. Aroma constituents of soybean [Glycine max (L.) Merri] milk lacking lipoxygenase isozymes. J. Agric. Food Chem. 43 : 2449-2452 https://doi.org/10.1021/jf00057a025
  19. Kramer, A. and W. H. Kwee. 1977. Functional and nutritional properties of tomato protein concentrate. J. Food Sci. 42: 207­-211 https://doi.org/10.1111/j.1365-2621.1977.tb01253.x
  20. Kumar, R., V. Choudhary, S. Mishra, I. K. Varma, and B. Mattia­son. 2002. Adhesives and plastics based on soy protein products. Ind. Crops & Prod. 16 : 155-172 https://doi.org/10.1016/S0926-6690(02)00007-9
  21. Lee, H. I., K. C. Kim, and E. H. Park. 2005. Sprout properties and lipoxygenase activity of lipoxygenase-Iess soybean genotypes. Korean J. Crop Sci. 50(S) : 112-117
  22. Mueller, I. N. 1992. Isolated soy proteins for surimi based prod­ucts. Protein Technol Int. A subsidiary of the Ralston Purina Company. Seoul, April, p. 21
  23. Nakai, S. J. 1983. Structure-function relationships offood proteins with an emphasis on the importance of protein hydrophobicity. J. Agric. Food Chem. 31 : 676-683 https://doi.org/10.1021/jf00118a001
  24. Narvel, J. M., W. R. Fehr, and L. C. Weldon. 2000. Ana]ysis of soybean seed lipoxygenases. Crop Sci. 40 : 838-840 https://doi.org/10.2135/cropsci2000.403838x
  25. Nishiba, Y. and I. Suda. 1998. Degradation of vitamin E, vitamin C and Lutein in soybean homogenate: A comparison of norma] soybean and lipoxygenase lacking (triple-null) soybean. J. Agric. Food Chem. 46 : 3708-3712 https://doi.org/10.1021/jf980350t
  26. Ortiz, S. E. M. and J. R. Wagner. 2002. Hydrolysates of native and modified soy protein isolates: structural characteristics, solubil­ity and foaming properties. Food Res. Int. 35 : 511-518 https://doi.org/10.1016/S0963-9969(01)00149-1
  27. Petruccelli, S. and M. C. Anon. 1995. Thermal aggregation of soy protein isolates. J. Agric. Food Chem. 43 : 3035-3041 https://doi.org/10.1021/jf00060a009
  28. Qi, M., N. S. Hettiarachchy, and U. Kalapathy. 1997. Solubility and emulsifying properties of protein isolates modified by pan­creatin. J. Food Sci. 62 : 1110-1115 https://doi.org/10.1111/j.1365-2621.1997.tb12224.x
  29. Richardson, T. 1977. Functional changes in proteins following action of enzymes. In: Feeney RE, Whitaker JR, editors. Food proteins: Improvement through chemical and enzymatic modi­fication. American chemical society, Washington DC. p. 185
  30. Saio, K. and T. Watanabe. 1973. Food use of soybean 7S and II Sprotein; Extraction and functional properties of their frac­tions. J. Food Sci. 38: 1139-1144 https://doi.org/10.1111/j.1365-2621.1973.tb07222.x
  31. Son, B. Y., Y. H. Lee, S. H. Kim, H. S. Lee, and S. H. Lee. 2002. Effects of planting date and accelerated aging on seed germina­tion-related traits of lipoxygenase-lacking soybean. Korean J. Crop Sci. 47: 196-200
  32. Sorgentini, D. A., J. R. Wagner, and M. C. Anon. 1995. Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions. J. Agric. Food Chem. 43: 2471-2479 https://doi.org/10.1021/jf00057a029
  33. Wagner, J. R., D. A. Sorgentini, and M. C. Anon. 2000. Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates. J. Agric. Food Chem. 48 : 3159-3165 https://doi.org/10.1021/jf990823b
  34. Were, L., N. S. Hettiarachchy, and U. Kalapathy. 1997. Modified soy proteins with improved foaming and water hydration prop­erties. J. Food Sci. 62 : 821-823, 850 https://doi.org/10.1111/j.1365-2621.1997.tb15463.x
  35. Wu, W. U., N. S. Hettiarachchy, and M. Qi. 1998. hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. J. Amer. Oil Chem. Soc. 75 : 845-850 https://doi.org/10.1007/s11746-998-0235-0
  36. Yamashita, M., S. Arai, J. Matsuyama, M. Gonda, H. Kato, and M. Fujimaki. 1970. Enzymatic modification of proteins in food­stuffs. Part Ill. Phenomenal survey on ${\alpha}$-chymotrypsin plastein synthesis from peptic hydrolysates of soy protein. Agric. BioI. Chem. 34: 1484-1491 https://doi.org/10.1271/bbb1961.34.1484