Effect of high pressure treatment on aggregation and structural properties of soy protein isolate

LWT

Volumn 42, Issue 2, 2009, Pages 606-611

  Tang, Chuan He ^a   Ma, Ching Yung ^b  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

^b UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

Fourier transform infrared (FTIR) spectroscopy; High pressure; Laser scattering; Protein conformation; Soy protein isolate (SPI)

Indexed keywords

AGGREGATES; HIGH PRESSURE EFFECTS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; STRUCTURAL PROPERTIES;

EFFECT OF HIGH PRESSURE; HIGH PRESSURE; HIGH-PRESSURE TREATMENT; INSOLUBLE AGGREGATES; LASER SCATTERING; MULTI ANGLE; PROTEIN CONFORMATION; SIZE-EXCLUSION CHROMATOGRAPHY; SOY PROTEIN ISOLATE; SOY PROTEIN ISOLATES;

FOURIER TRANSFORM INFRARED SPECTROSCOPY;

GLYCINE MAX;

EID: 55549102634     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2008.07.012     Document Type: Article

References (29)

1. Allain A.-F., Paquin P., and Subirade M. Relationship between conformation of β-lactoglobulin in solution and gel states as revealed by attenuated total reflection fourier transform infrared spectroscopy. International Journal of Biological Macromolecules 26 (1999) 337-344
2. Apichartsrangkoon A. Effects of high pressure on rheological properties of soy protein gels. Food Chemistry 80 (2003) 55-60
3. Boye J.I., Ismail A.A., and Alli I. Effects of physicochemical factors on the secondary structure of β-lactoglobulin. Journal of Dairy Research 63 (1995) 97-109
4. Boye J.I., Ma C.Y., and Ismail A.A. Thermal denaturation and gelation characteristics of β-lactoglobulin genetic variants. Functional properties of proteins and lipids (1998), American Chemical Society, Washington, DC
5. Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
6. Chapleau N., and de Lamballerie-Anton M. Improvement of emulsifying properties of lupin proteins by high pressure induced aggregation. Food Hydrocolloids 17 (2003) 273-280
7. Choi S.M., and Ma C.-Y. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry. Journal of Agricultural and Food Chemistry 53 (2005) 8046-8053
8. Choi S.-W., and Ma C.-Y. Study of Thermal Aggregation of Globulin from Common Buckwheat (Fagopyrum esculentum Moench) by Size-Exclusion Chromatography and Laser Light Scattering. Journal of Agricultural and Food Chemistry 54 (2006) 554-561
9. Clark A.H., Saunderson D.H., and Suggett A. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. International Journal of Peptide and Protein Research 17 (1981) 353-364
10. Dzwolak W., Kato M., Shimizu A., and Taniguchi Y. Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: the stabilizing role of the calcium ion. Biochimica et Biophysica Acta 1433 (1999) 45-55
11. Ellepola S.W., Choi S.M., and Ma C.-Y. Conformational study of globulin from rice (Oryza sativa) seeds by fourier-transform infrared spectroscopy. International Journal of Biological Macromolecules 37 (2005) 12-20
12. Hoffman M.A.M., Sala G., Olieman C., and de Kruif C.G. Molecular mass distributions of heat-induced β-lactoglobulin aggregate. Journal of Agricultural and Food Chemistry 45 (1997) 2945-2957
13. Lefèvre T., and Subirade M. Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers 54 (2000) 578-586
14. Lefèvre T., and Subirade M. Molecular structure and interaction of biopolymers as viewed by fourier transform infrared spectroscopy: model studies on β-lactoglobulin. Food Hydrocolloids 15 (2001) 365-376
15. Militello V., Casarino C., Emanuele A., Giostra A., Pullara F., and Leone M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophysical Chemistry 107 (2004) 175-187
16. Mine Y. Laser light scattering study on the heat-induced ovalbumin aggregates related to its gelling property. Journal of Agricultural and Food Chemistry 44 (1996) 2086-2090
17. Molina E., Papadopoulou A., and Ledward D.A. Emulsifying properties of high pressure treated soy protein isolates and 7S and 11S globulins. Food Hydrocolloids 15 (2001) 263-269
18. Plietz P., Drescher B., and Damaschun G. Relationship between the amino acid sequence and the domain structure of the subunits of the 11S seed globulins. International Journal of Biological Macromolecule 9 (1987) 161-165
19. 10-helices in globular proteins. International Journal of Peptide and Protein Research 37 (1991) 508-512
20. Puppo C., Chapleau N., Speroni F., de Lamballerie-Anton M., Michel F., Añón C., et al. Physicochemical modifications of high-pressure-treated soybean protein isolates. Journal of Agricultural and Food Chemistry 52 (2004) 1564-1571
21. Puppo M.C., Speroni F., Chapleau N., de Lamballerie M., Añón M.C., and Anton M. Effect of high-pressure treatment on emulsifying properties of soybean proteins. Food Hydrocolloids 19 (2005) 289-296
22. Schokker E.P., Singh H., Pinder D.N., Norris G.E., and Creamer L.K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. International Dairy Journal 9 (1999) 791-800
23. Subirade M., Gueguen J., and Pézolet M. Conformational changes upon dissociation of a globular protein from pea: a Fourier transform infrared spectroscopy study. Biochimica et Biophysica Acta 1205 (1994) 239-247
24. Susi H., and Byler D.M. Fourier transform infrared spectroscopy in protein conformation studies. In: Cherry J.P., and Barford R.A. (Eds). Methods for protein analysis (1988), American Oil Chemists' Society, Champaign, IL
25. Tang C.H., and Ma C.Y. Modulation of the thermal stability of β-lactoglobulin by means of microbial transglutaminase treatment. European Food Research and Technology 225 (2007) 649-652
26. Wang X.S., Tang C.H., Li B.S., Yang X.Q., Li L., and Ma C.Y. Effects of high pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloids 22 (2008) 560-567
27. Wyatt P.J. Light scattering and absolute characterization of macromolecules. Analytical Chimica Acta 272 (1993) 1-40
28. Zhang H.K., Li L.T., Tatsumi E., and Kotwal S. Influence of high pressure on conformational changes of soybean glycinin. Innovative Food Science and Emerging Technologies 4 (2003) 269-275
29. 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