Thermal aggregation and gelation of kidney bean (Phaseolus vulgaris L.) protein isolate at pH 2.0: Influence of ionic strength

Food Hydrocolloids

Volumn 24, Issue 4, 2010, Pages 266-274

  Zhang, Ye Hui ^a   Tang, Chuan He ^a,b   Wen, Qi Biao ^a   Yang, Xiao Quan ^a   Li, Lin ^a   Deng, Wen Li ^a  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

^b South China University of Technology   (China)

Author keywords

Electrostatic interactions; Fibrillar gels; Kidney bean protein isolate; Percolation model; Thermal aggregation

Indexed keywords

ATOMIC FORCE MICROSCOPY; DYNAMIC LIGHT SCATTERING; ELECTROSTATICS; FRACTALS; GELATION; GELS; IONIC STRENGTH; PROTEINS; TURBIDITY;

ATOMIC-FORCE-MICROSCOPY; DYNAMIC LIGHT-SCATTERING; DYNAMIC-LIGHT SCATTERINGS; FIBRILLAR GEL; KIDNEY BEAN PROTEIN ISOLATE; KIDNEY BEANS; PERCOLATION MODELS; PROTEIN ISOLATES; THERMAL AGGREGATION; THERMAL GELATION;

SOLVENTS;

PHASEOLUS VULGARIS;

EID: 75149122292     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2009.10.002     Document Type: Article

References (30)

1. Akkermans C., van der Goot A.J., Venema P., Vereijken J.M., van der Linden E., and Boom R.M. Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate. Journal of Agricultural and Food Chemistry 55 (2007) 9877-9882
2. AOAC. Official methods of analysis. 14th ed. (1985), Association of Official Analytical Chemists, Washington DC
3. Arnaudov L.N., de Vries R., Ippel H., and Mierlo C.P.M. Multiple steps during the formation of β-lactogloblin fibrils. Biomacromolecules 4 (2003) 1614-1632
4. Arntfield S.D., and Murray E.D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Canadian Institute of Food Science and Technology Journal 14 (1981) 289-294
5. Aymard P., Nicolai T., and Durand D. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 32 (1999) 2542-2552
6. Ikeda S., and Morris V. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3 (2002) 382-389
7. Ikeda S., Morris V.J., and Nishinari K. Microstructure of aggregated and nonaggregated k-carrageenan helices visualized by atomic force microscopy. Biomacromolecules 2 (2001) 1331-1337
8. Jachimska B., Wasilewska M., and Adamczyk Z. Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 24 (2008) 6866-6872
9. Kavanagh G.M., Clark A.H., and Ross-Murphy S.B. Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels. International Journal of Biological Macromolecules 28 (2000) 41-50
10. Kimura A., Fukuda T., Zhang M., Motoyama S., Maruyama N., and Utsumi S. Comparison of physicochemical properties of 7S and 11S globulins from pea, Fava bean, cowpea and French bean with those of soybean - French bean 7S globulin exhibits excellent properties. Journal of Agricultural and Food Chemistry 56 (2008) 10273-10279
11. Kristjansson M.M., and Kinsella J.E. Protein and enzyme stability:structural, thermodynamic, and experimental aspects. Advance in Food Nutrition Research 35 (1991) 237-316
12. Kroy K., and Frey E. Force-extension relation and plateau modulus for wormlike chains. Physics Review Letters 77 (1996) 306-309
13. Le Bon C., Nicolai T., and Durand D. Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32 (1999) 6120-6127
14. van der Linden E., and Sagis L.M.C. Isotropic force percolation in protein gels. Langmuir 17 (2001) 5821-5824
15. MacKintosh F.C., Käs J., and Janmey P.A. Elasticity of semiflexible biopolymer networks. Physics Review Letters 75 (1995) 4425-4431
16. Meng G.-T., and Ma C.-Y. Thermal properties of Phaeolus angularis (red bean) globulin. Food Chemistry 73 (2001) 453-460
17. Mori T., Nakamura T., and Utsumi S. Behavior of intermolecular bond formation in the late stage of heat-induced gelation of glycinin. Journal of Agricultural and Food Chemistry 34 (1986) 33-36
18. Morris V.J., Mackie A.R., Wilde P.J., Kirby A.R., Mills E.C., and Gunning A.P. Atomic force microscopy as a tool for interpreting the rheology of food biopolymers at the molecular level. Lebensmittel-Wissenschaft und-Technologie 34 (2001) 3-10
19. Sagis L.M.C., Veerman C., Ganzevles R., Ramaekers M., Bolder S.G., and van der Linden E. Mesoscopic structure and viscoelastic properties of β-lactoglobulin gels at low pH and low ionic strength. Food Hydrocolloids 16 (2002) 207-213
20. Tang C.H. Thermal denaturation and gelation of vicilin-rich protein isolates from three Phaseolus legumes: a comparative study. LWT-Food Science and Technology 41 (2008) 1380-1388
21. Tang C.H., Chen L., and Ma C.Y. Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: a comparative study. Food Chemistry 113 (2009) 957-963
22. Tang C.H., Sun X., and Yin S.W. Physicochemical, functional and structural properties of vicilin-rich protein isolate from three Phaseolus legumes: effect of heat treatment. Food Hydrocolloids 23 (2009) 1771-1778
23. Tobitani A., and Ross-Murphy S.B. Heat-induced gelation of globular proteins. 1. Model for the effects of time and temperature on the gelation time of BSA gels. Macromolecules 30 (1997) 4845-4854
24. Vardhanabhuti B., and Foegeding E.A. Effects of dextran sulfate, NaCl, and initial protein concentration on thermal stability of β-lactoglobulin and α-lactalbumin at neutral pH. Food Hydrocolloids 22 (2008) 752-762
25. Veerman C., Ruis H., Sagis L.M.C., and van der Linden E. Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactogloblin gels. Biomacomolecules 3 (2002) 869-873
26. Veerman C., Sagis L.M.C., Heck J., and van der Linden E. Mesostructure of fibrillar bovine serum albumin gels. International Journal of Biological Macromolecules 31 (2003) 139-146
27. Weijers M., Sagis L.M.C., Veerman C., Sperber B., and van der Linden E. Rheology and structure of ovalbumin gels at low pH and low ionic strength. Food Hydrocolloids 16 (2002) 269-276
28. Yang H., Wang Y., Lai S., An H., Li Y., and Chen F. Application of atomic force microscopy as a nanotechnology tool in food science. Journal of Food Science 72 (2007) R65-R75
29. Yin S.W., Tang C.H., Wen Q.B., Yang X.Q., and Li L. Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: effect of high-pressure treatment. Food Chemistry 110 (2008) 938-945
30. Zhao Y., Mine Y., and Ma C.-Y. Study of thermal aggregation of oat globulin by laser light scattering. Journal of Agricultural and Food Chemistry 52 (2004) 3089-3096