pH-Induced Modifications in the Thermal Stability of Soybean Protein Isolates

Journal of Agricultural and Food Chemistry

Volumn 44, Issue 10, 1996, Pages 3005-3009

  Petruccelli, Silvana ^a   Añón, María Cristina ^a  

^a Facultad de Ciencias Naturales e Instituto M Lillo   (Argentina)

Author keywords

Denaturation; Globulin; Soybean; Thermal stability

Indexed keywords

GLYCINE MAX;

EID: 0000229101     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9600061     Document Type: Article

References (32)

1. Arntfield, S. D.; Murray, E. D. The influence of processing parameters on food protein functionality. I. Differential Scanning Calorimetry as an Indicator of Protein Denaturation. Can. Inst. Food Sci. Technol. J. 1981, 14, 289-294.
2. Badley, R. A.; Atkinson, D.; Hauser, H.; Oldani, D.; Green, J. P.; Stubbs, J. M. The structure, physical and chemical properties of the soy bean protein glycinin. Biochim. Biophys. Acta 1975, 412, 214-228.
3. Borchardt, H. J.; Daniels, F. The application of differential thermal analysis to the study of reaction kinetics. J. Amer. Chem. Soc. 1957, 79, 41-46.
4. Damodaran, S. Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation. J. Agric. Food Chem. 1988, 36, 262-269.
5. Das, K. P.; Kinsella, J. E. Stability of food emulsions: physicochemical role of protein and nonprotein emulsifiers. Adv. Food Nutr. Res. 1990, 34, 81-201.
6. Harwalkar, V. R.; Ma, C. Y. Study of thermal properties of oat globulin by differential scanning calorimetry. J. Food Sci. 1987, 52, 394-398.
7. Hayakawa, S.; Nakai, S. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci. 1985a, 50, 486-491.
8. Hayakawa, S.; Nakai, S. Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 1985b, 18, 290-295.
9. Hohlberg, A. I.; Stanley, D. W. Kinetics of bean protein thermal denaturation. J. Food Process. Preserv. 1987, 11, 31-42.
10. Iwabuchi, S.; Watanabe, H.; Yamauchi, F. Thermal denaturation of β-Conglycinin. Kinetic resolution of reaction mechanism. J. Agric. Food Chem. 1991a, 39, 27-33.
11. Iwabuchi, S.; Watanabe, H.; Yamauchi, F. Observations on the dissociation of β-Conglycinin into subunits by heat treatment. J. Agric. Food Chem. 1991b, 39, 34-40.
12. Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
13. Kato, A.; Tsutsui, N.; Matsudomi, N.; Kobayashi, K.; Nakai, S. Effects of partial denaturation on surface properties of ovalbumin and lysozyme. Agric. Biol. Chem. 1981, 45, 2755-2760.
14. Kato, A.; Osako, Y.; Matsudomi, N.; Kobayashi, K. Changes in the emulsifying and foaming properties of proteins during heat denaturation. Agric. Biol. Chem. 1983, 47, 33-38.
15. Kato, A.; Yamaoka, H.; Matsudomi, N.; Kobayashi, K. Functional properties of cross-linked lysozyme and serum albumin. J. Agric. Food Chem. 1986, 34, 370-372
16. Kinsella, J. E. Functional properties of soy proteins. J. Am. Oil Chem. Soc. 1979, 56, 242-258.
17. Lowry, O. H.; Rosebrough, N. J.; Farr, A. L.; Randall, R. J. Protein measurement with the folin-phenol reagent. J. Biol. Chem. 1951, 193, 265-275.
18. Ma, C. Y.; Harwalkar, V. R.; Paquet, A. Physicochemical properties of alkali-treated oat globulin. J. Agric. Food Chem. 1990, 38, 1707-1711.
19. Matsudomi, N.; Mori, H.; Kato, A.; Kobayashi, K. Emulsifying and foaming properties of heat denatured soybean 11S globulins in relation to their surface hydrophobicity. Agric. Biol. Chem. 1985, 49, 915-919.
20. Nielsen, N. C. The structure and complexity of the 11S polypeptides in soybeans. J. Am.. Oil Chem. Soc. 1985, 62, 1680-1686.
21. Ozawa, T. Kinetic analysis of derivative curves in thermal analysis. J. Therm. Anal. 1970, 2, 301-324.
22. Petruccelli, S.; Añón, M. C. The relationship between the method of obtention and the structural and functional properties of soy protein isolates. Part II: Surface properties. J. Agric. Food Chem. 1994, 42, 2170-2176.
23. Petruccelli, S.; Añón, M. C. Partial reduction of soy protein isolate disulfide bonds. J. Agric. Food Chem. 1995a, 43, 2001-2006.
24. Petruccelli, S.; Añón, M. C. Thermal aggregation of soy protein isolates. J. Agric. Food Chem. 1995b, 43, 3035-3041.
25. Shimizu, M.; Saito, M.; Yamauchi, K. Hydrophobicity and emulsifying activity of milk proteins. Agric. Biol. Chem. 1986, 50, 791-792.
26. Thanh, V. H.; Shibasaki, K. Major proteins of soybeans seeds. Reversible and irreversible dissociation of conglycinin. J. Food Agric. Food Chem. 1979, 27, 805-809.
27. Townsend, A. A.; Nakai, S. Relationships between hydrophobicity and foaming characteristics of food proteins. J. Food Sci. 1983, 48, 588-594.
28. Voutsinas, L. P.; Cheung, E.; Nakai, S. Relationships of hydrophobicity to emulsifying properties of heat denatured proteins. J. Food Sci. 1983a, 48, 26-32.
29. Voutsinas, L. P.; Nakai, S.; Harwalkar, V. R. Relationshpis between protein hydrophobicity and thermal functional properties of food proteins. Can. Inst. Food Sci. Technol. J. 1983b, 16, 185-190.
30. Watanabe, K. Kinetics of the heat insolubilisation of soybean 11S globulin in a phosphate buffer system. Agric. Biol.Chem. 1988, 52, 2095-2096.
31. Wolf, W. J. Purification and properties of the proteins. In Soybeans: Chemistry and Technology; Smith, A. K., Circle, S. J., Eds.; AVI Publishing Co.: Westport, CT, 1978; pp 93-143.
32. Wolf, W. J.; Briggs, D. R. Ultracentrifugal investigation of the effect of neutral salts on the extraction of soybean proteins. Arch. Biochem. Biophys. 1956, 63, 40-49.