Limited aggregation behavior of β-conglycinin and its terminating effect on glycinin aggregation during heating at pH 7.0

Journal of Agricultural and Food Chemistry

Volumn 60, Issue 14, 2012, Pages 3782-3791

  Guo, Jian ^a   Yang, Xiao Quan ^a   He, Xiu Ting ^a   Wu, Na Na ^a   Wang, Jin Mei ^a   Gu, Wei ^a   Zhang, Yuan Yuan ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

conglycinin; glycinin; insoluble aggregates; soluble aggregates; soy protein; thermal aggregation

Indexed keywords

CONGLYCININ; GLYCININ; SOLUBLE AGGREGATES; SOY PROTEIN; THERMAL AGGREGATION;

AGGLOMERATION; PH EFFECTS; SOLUBILITY;

AGGREGATES;

BETA CONGLYCININ PROTEIN, GLYCINE MAX; BETA-CONGLYCININ PROTEIN, GLYCINE MAX; GLOBULIN; GLYCININ; PLANT ANTIGEN; SEED STORAGE PROTEIN; SOYBEAN PROTEIN;

ARTICLE; CHEMICAL PHENOMENA; CHEMISTRY; GEL CHROMATOGRAPHY; HEAT; LIGHT; PARTICLE SIZE; PH; PROTEIN FOLDING; RADIATION SCATTERING; SOLUBILITY;

ANTIGENS, PLANT; CHROMATOGRAPHY, GEL; GLOBULINS; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGHT; PARTICLE SIZE; PROTEIN FOLDING; SCATTERING, RADIATION; SEED STORAGE PROTEINS; SOLUBILITY; SOYBEAN PROTEINS;

EID: 84859602716     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf300409y     Document Type: Article

References (50)

1. Duranti, M.; Lovati, M. R.; Dani, V.; Barbiroli, A.; Scarafoni, A.; Castiglioni, S.; Ponzone, C.; Morazzoni, P. The α′ subunit from soybean 7S globulin lowers plasma lipids and upregulates liver β-VLDL receptors in rat feed a hypercholesterolemic diet J. Nutr. 2004, 134, 1334-1339
2. Moriyama, T.; Kishimoto, K.; Nagai, K.; Urade, R.; Ogawa, T.; Utsumi, S.; Maruyama, N.; Maebuchi, M. Soybean β-conglycinin diet suppresses serum triglyceride levels in normal and genetically obese mice by induction of β-oxidation, downregulation of fatty acid synthase, and inhibition of triglyceride absorption Biosci., Biotechnol., Biochem. 2004, 68, 352-359
3. Martinez-Villaluenga, C.; Bringe, N. A.; Berhow, M. A.; Gonzalez de Mejia, E. β-Conglycinin embeds active peptides that inhibit lipid accumulation in 3T3-L1 adipocytes in vitro J. Agric. Food Chem. 2008, 56, 10533-10543
4. Wilgus, H. S., Jr.; Norris, L. C.; Heuser, O. F. Effect of heat on nutritive value of soybean oil meal Ind. Eng. Chem. 1936, 28, 586-588
5. Keerati-u-rai, M.; Corredig, M. Heat-induced change in oil-in-water emulsion stabilized with soy protein isolate Food Hydrocolloids 2009, 23, 2141-2148
6. Sorgentini, D. A.; Wagner, J. R.; Añón, M. C. Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions J. Agric. Food Chem. 1995, 43, 2471-2479
7. Guo, J.; Zhang, Y.; Yang, X.-Q. A novel enzyme cross-linked gelation method for preparing food globular protein-based transparent hydrogel Food Hydrocolloids 2012, 26, 277-285
8. Kinsella, J. E. Functional properties of soy proteins J. Am. Oil Chem. Soc. 1979, 56, 242-258
9. Wolf, W. J.; Babcock, G. E.; Smith, A. K. Ultracentrifugal differences in soybean protein composition Nature 1961, 191, 1395-1396
10. Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds. Subunit structure of β-conglycinin J. Agric. Food Chem. 1978, 26, 692-695
11. Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds. Reconstitution of β-conglycinin from its subunits J. Agric. Food Chem. 1978, 26, 695-698
12. Badley, R. A.; Atkinson, D.; Hauser, H.; Oldan, 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
13. Moreira, M. A.; Hermodson, M. A.; Larkins, B. A.; Nielsen, N. C. Comparison of the primary structure of the acidic polypeptides of glycinin Arch. Biochem. Biophys. 1981, 210, 633-642
14. Staswick, P. E.; Hermodson, M. A.; Nielsen, N. C. Identification of the acidic and basic subunit complexes of glycinin J. Biol. Chem. 1981, 256, 8752-8755
15. Wolf, W. J.; Tamura, T. Heat denaturation of soybean 11S protein Cereal Chem. 1969, 46, 331-344
16. Hashizume, K.; Watanabe, T. Influence of heating temperature on conformational changes of soybean proteins Agric. Biol. Chem. 1979, 43, 683-690
17. Kuipers, B. J. H.; Gruppen, H. Identification of strong aggregating regions in soy glycinin upon enzymatic hydrolysis J. Agric. Food Chem. 2008, 56, 3818-3827
18. Damodaran, S.; Kinsella, J. E. Effect of conglycinin on the thermal aggregation of glycinin J. Agric. Food Chem. 1982, 30, 812-817
19. German, B.; Damodaran, S.; Kinsella, J. E. Thermal dissociation and association behavior of soy proteins J. Agric. Food Chem. 1982, 30, 807-811
20. Yamagishi, T.; Miyakawa, A.; Noda, N.; Yamauchi, F. Isolation and electrophoretic analysis of heat-induced of mixed soybean 7S and 11S globulins Agric. Biol. Chem. 1983, 47, 1229-1237
21. Utsumi, S.; Damodaran, S.; Kinsella, J. E. Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and β subunits of 7S J. Agric. Food Chem. 1984, 32, 1406-1412
22. Utsumi, S.; Kinsella, J. E. Structure-function relationships in food proteins: subunit interactions in heat-induced gelation of 7S, 11S, and soy isolate proteins J. Agric. Food Chem. 1985, 33, 297-303
23. Petruccelli, S.; Añón, M. C. Thermal aggregation of soy protein isolates J. Agric. Food Chem. 1995, 43, 3035-3041
24. Keerati-u-rai, M.; Corredig, M. Heat-induced changes occurring in oil/water emulsions stabilized by soy glycinin and β-conglycinin J. Agric. Food Chem. 2010, 58, 9171-9180
25. Roberts, C. J. Non-native protein aggregation kinetics Biotechnol. Bioeng. 2007, 98, 927-938
26. Andrews, J. M.; Roberts, C. J. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics. 1. Aggregation with pre-equilibrated unfolding J. Phys. Chem. B 2007, 111, 7897-7913
27. Li, Y.; Roberts, C. J. Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization J. Phys. Chem. B 2009, 113, 7020-7032
28. Andrews, J. M.; Roberts, C. J. Non-native aggregation of α-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies Biochemistry 2007, 46, 7558-7571
29. Andrews, J. M.; Weiss, W. F., IV; Roberts, C. J. Nucleation, growth, and activation energies for seeded and unseeded aggregation of α- chymotrypsinogen A Biochemistry 2008, 47, 2397-2403
30. Li, Y.; Weiss, W. F., IV; Roberts, C. J. Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering J. Pharm. Sci. 2009, 98, 3997-4016
31. Li, Y.; Ogunnaike, B. A.; Roberts, C. J. Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for α-chymotrypsinogen A J. Pharm. Sci. 2010, 99, 645-662
32. Weiss, W. F., IV; Hodgdon, T. K.; Kaler, E. W.; Lenhoff, A. M.; Roberts, C. J. Nonnative protein polymers: structure, morphology, and relation to nucleation and growth Biophys. J. 2007, 93, 4392-4403
33. Brummitt, R. K.; Nesta, D. P.; Chang, L.; Chase, S. F.; Laue, T. M.; Roberts, C. J. Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. Unfolding, colloidal interactions, and formation of high-molecular- weight aggregates. J. Pharm. Sci. 2011, 100, 2087-2103.
34. Brummitt, R. K.; Nesta, D. P.; Chang, L.; Kroetsch, A. M.; Roberts, R. J. Nonnative aggregation of an IgG1 antibody in acidic conditions: part 2. Nucleation and growth kinetics with competing growth mechanisms J. Pharm. Sci. 2011, 100, 2104-2119
35. Rao, G.; Iyer, V.; Kosloski, M. P.; Pisal, D. S.; Shin, E.; Middaugh, C. R.; Balu-Iyer, S. V. Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics J. Pharm. Sci. 2010, 99, 1697-1706
36. Nagano, T.; Hirotsuka, M.; Mori, H.; Kohyama, K.; Nishinari, K. Dynamic viscoelastic study on the gelation of 7S globulin from soybeans J. Agric. Food Chem. 1992, 40, 941-944
37. Lowry, O. H.; Rosebrough, N. J.; Farr, A. L.; Randall, O. J. Protein measurement with the folin phenol reagent J. Biol. Chem. 1951, 193, 265-275
38. Liu, X. M.; Powers, J. R.; Swanson, B. G.; Hill, H. H.; Clark, S. Modification of whey protein concentrate hydrophobicity by high hydrostatic pressure Innovative Food Sci. Emerging Technol. 2005, 6, 310-317
39. 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
40. Anderson, R. L. Effects of steaming on soybean proteins and trypsin inhibitors J. Am. Oil Chem. Soc. 1992, 69, 1170-1176
41. Petruccelli, S.; Añón, M. C. pH-Induced modifications in the thermal stability of soybean protein isolates J. Agric. Food Chem. 1996, 44, 3005-3009
42. Sorgentini, D. A.; Wagner, J. R. Comparative study of structural characteristics and thermal behavior of whey and isolate soybean proteins J. Food Biochem. 1999, 23, 489-507
43. Renkema, J. M. S.; van Vliet, T. Heat-induced gel formation by soy proteins at neutral pH J. Agric. Food Chem. 2002, 50, 1569-1573
44. Burchard, W. Solution properties of branched macromolecules Adv. Polym. Sci. 1999, 143, 113-193
45. Schmitt, C.; Moitzi, C.; Bovay, C.; Rouvet, M.; Bovetto, L.; Donato, L.; Leser, M. E.; Schurtenberger, P.; Stradner, A. Internal structure and colloidal behaviour of covalent whey protein microgels obtained by heat treatment Soft Matter 2010, 6, 4876-4884
46. Receveur-Bréchot, V.; Bourhis, J. M.; Uversky, V. N.; Canard, B.; Longhi, S. Assessing protein disorder and induced folding Proteins: Struct., Funct., Bioinf. 2006, 62, 24-45
47. Maruyama, N.; Katsube, T.; Wada, Y.; Oh, M. H.; Barba De La Rosa, A. P.; Okuda, E.; Nakagawa, S.; Utsumi, S. The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features Eur. J. Biochem. 1998, 258, 854-862
48. Maruyama, N.; Sato, R.; Wada, Y.; Matsumura, Y.; Goto, H.; Okuda, E.; Nakagawa, S.; Utsumi, S. Structure-physicochemical function relationships of soybean β-conglycinin constituent subunits J. Agric. Food Chem. 1999, 47, 5278-5284
49. Yuan, D.-B.; Yang, X.-Q.; Tang, C.-H.; Zheng, Z.-X.; Min, W.; Ahmad, I.; Yin, S.-W. Physicochemical and functional properties of acidic and basic polypeptides of soy glycinin Food Res. Int. 2009, 42, 700-706
50. Iwabuchi, S.; Watanabe, H.; Yamauchi, F. Thermal denaturation of β-conglycinin. Kinetic resolution of reaction mechanism J. Agric. Food Chem. 1991, 39, 27-33