Relationship Between Surface Hydrophobicity and Structure of Soy Protein Isolate Subjected to Different Ionic Strength

REFERENCES

• Vakhtang, V.L.; Dmitri, N.E.; George, I.M. Thermodynamic consequences of rurial of polar and non-polar amino acid residues in the protein interior. Journal of Molecular Biology 2002, 320, 343–357.
   PubMed Web of Science ®Google Scholar
• Shuryo, N. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. Journal of Agricultural and Food Chemistry 1983, 31, 676–683.
   Web of Science ®Google Scholar
• Jiang, J.; Xiong, Y.L.; Chen, J. Roll of β-conglycinin and glycinin sunbunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate. Journal of Food Science 2011, 76, 293–302.
   Web of Science ®Google Scholar
• Herreroa, A.M.; Carmonab, P.; Pintadoa, T.; Jimenz-Comlmeneroa, F.; Ruiz-Capillasa, C. Infrared spectroscopic analysis of structural features and interactions in olive oil-in-water emulsions stabilized with soy protein. Food Research International 2011, 44, 360–366.
   Web of Science ®Google Scholar
• Zhang, Y.N.; Zhao, X.H. Study on the functional properties of soybean protein isolate cross-linked with gelatin by microbial transglutaminase. International Journal of Food Properties 2013, 6 (16), 1257–1270.
   Web of Science ®Google Scholar
• Romero, A.; Cordobés, F.; Guerrero, A.; Puppo, M.C. Influence of protein concentration on the properties of crayfish protein isolated gels. International Journal of Food Properties 2014, 2 (17), 249–260.
   Web of Science ®Google Scholar
• Benoit, S. M.; Nor Afizah, M.; Ruttarattanamongkol, K.; Rizvi, S.S.H. Effect of pH and temperature on the viscosity of texturized and commercial whey protein dispersions. International Journal of Food Properties 2013, 2 (16), 322–330.
   Web of Science ®Google Scholar
• Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta (BBA)—Protein Structure 1980, 624, 13–20.
   PubMed Web of Science ®Google Scholar
• Wagner, J.R.; Sorgentini, D.A.; Anon, M.C. Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates. Journal of Agricultural and Food Chemistry 2000, 48, 3159–3165.
   PubMed Web of Science ®Google Scholar
• Boatright, W.L.; Heltlarachchy, N.S. Soy protein isolate solubility and surface hydrophobicity as affected by antioxidants. Journal of Food Science 1995, 60, 798–801.
   Web of Science ®Google Scholar
• Townsend, A.A.; Nakai, S. Relationships between hydrophobicity and foaming characteristics of food proteins. Journal of Food Science 1983, 48, 588–594.
   Web of Science ®Google Scholar
• Wagner, J.R.; Gueguen, J. Surface functional properties of native, acid-treated, and reduced soy glycinin. 2. Emulsifying properties. Journal of Agricultural and Food Chemistry 1999, 47, 2181–2187.
   PubMed Web of Science ®Google Scholar
• Hettiarachchy, N.S.; Kalapathy, U.; Myers, D.J. Alkali-modified soy protein with improved adhesive and hydrophobic properties. Journal of the American Oil Chemists’ Society 1995, 72, 1461–1464.
   Web of Science ®Google Scholar
• Jiang, Y.; Tang, C.H.; Wen, Q.B.; Li, L.; Yang, X.Q. Effect of processing parameters on the properties of transglutaminase-treated soy protein isolate films. Innovative Food Science and Emerging Technologies 2007, 8, 218–225.
   Web of Science ®Google Scholar
• Wang, J.B.; Xia, N.; Yang, X.Q.; Yin, S.W.; Qi, J.R.; He, X.T.; Yuan, D.B.; Wang, L.J. Adsorption and dilatational rheology of heat-treated soy protein at the oil-water interface: relationship to structural properties. Journal of Agricultural and Food Chemistry 2012, 60, 3302–3310.
   PubMed Web of Science ®Google Scholar
• Parris, N.; Bardord, R. Interactions of Food Proteins; ACS Symposium Series 454. American Chemical Society: New York, 1991; 42–58.
   Google Scholar
• Aider, M.; Djename, D.; Ounis, W.B. Amino acid composition, foaming, emulsifying properties and surface hydrophobicity of mustard protein isolate as affected by pH and NaCl. International Journal of Food Science and Technology 2012, 47, 1028–1036.
   Web of Science ®Google Scholar
• Hu, H.; Wu, J.H.; Li-Chan, C.Y.E.; Zhu, L.; Zhang, F.; Xu, X.Y.; Fan, G.; Wang, L.F.; Huang, X.J.; Pan, S.Y. Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids 2012, 30, 647–655.
   Web of Science ®Google Scholar
• Shen, L.; Tang, C.H. Microfluidization as a potential technique to modify surface properties of soyprotein isolate. Food Research International 2012, 48, 108–118.
   Web of Science ®Google Scholar
• McMindes, M.K. Applications of isolated soy protein in low-fat meat products. Food Technology 1991, 45, 61–64.
   Web of Science ®Google Scholar
• Kimberly, L.J.; Charles, R.M. Protein and humic acid adsorption onto hydrophilic membrane surfaces: Effects of pH and ionic strength. Journal of Membrane Science 2000, 165, 31–46.
   Web of Science ®Google Scholar
• Boye, J.I.; Alli, I.; Ismail, A.A.; Gibbs, B.F.; Konishi, Y. Factors affecting molecular characteristics of whey protein gelation. International Dairy Journal 1995, 5, 337–353.
   Web of Science ®Google Scholar
• Bryant, C.M.; McClements, D.J. Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein. Journal of Food Science 2000, 65, 801–804.
   Web of Science ®Google Scholar
• Speroni, F.; Anon, M.C.; Lamballerie, M. Effects of calcium and high pressure on soybean proteins: A calorimetric study. Food Research International 2010, 43, 1347–1355.
   Web of Science ®Google Scholar
• Lowry, O.H.; Rosembroug, H.J., Lewis, A.; Randall, R.J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 1951, 193, 265–275.
   PubMed Web of Science ®Google Scholar
• Sreerama, N.; Venyaminov, S.Y.U.; Woody, R.W. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Science 1999, 8, 370–380.
   PubMed Web of Science ®Google Scholar
• McClements, D.J. Food Emulsions: Principles, Practice, and Techniques; CRC Press: Boca Raton, FL, 1999.
   Google Scholar
• Shigeru, H.; Shuryo, N. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 1985, 50, 486.
   Web of Science ®Google Scholar
• Moure, A.; Sineiro, J.; Dominguez, H.; Parajo, J.C. Functionality of oilseed protein products: A review. Food Research International 2006, 39, 945–963.
   Web of Science ®Google Scholar
• Kalapathy, U.; Hettiarachchy, N.S.; Rhee, K.C. Effect of drying methods on molecular properties and functionalities of disulfide bond-cleaved soy proteins. Journal of the American Oil Chemists’ Society 1997, 74, 195–199.
   Web of Science ®Google Scholar
• Renkema, J.M.S., Gruppen, H.; Vliet, T. Influence of pH and ionic strength on heat-induced formation and rheological properties of soy protein gels in relation to denaturation and their protein compositions. Journal of Agricultural and Food Chemistry 2002, 50, 6064–6071.
   PubMed Web of Science ®Google Scholar
• Kalapathy, U.; Hettiarachchy, N.S.; Myers, D.; Rhee, K.C. Alkali-modified soy proteins: Effect of salts and disulfide bond cleavage on adhesion and viscosity. Journal of the American Oil Chemists’ Society 1996, 73, 1063–1066.
   Web of Science ®Google Scholar
• Hogg, P.J. Disulfide bonds as switches for protein function. Trends in Biochemical Sciences 2003, 28, 210–214.
   PubMed Web of Science ®Google Scholar
• Chen, Y.; Barkley, M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 1998, 37, 9976–9982.
   PubMed Web of Science ®Google Scholar
• Vivian, J.T.; Callis, P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophysical Journal 2001, 80, 2093–2109.
   PubMed Web of Science ®Google Scholar
• Przybycien, T.M.; Bailey, J.E. Secondary structure perturbations in salt-induced protein precipitates. Biochimica et Biophysica Acta (BBA)—Protein Structure 1991, 1076, 103–111.
   PubMed Web of Science ®Google Scholar
• Hopp, T.P. Protein surface analysis: methods for identifying antigenic determinants and other interaction sites. Journal of Immunological Methods 1986, 88, 1–18.
   PubMed Web of Science ®Google Scholar
• Fennema, O.R. Food Chemistry; Marcel Dekker Inc.: New York, 1996; 321–429.
   Google Scholar
• Smith, J.S.; Scholtz, J.M. Energetics of polar side-chain interactions in helical peptides: Salt effects on ion pairs and hydrogen bonds. Biochemistry 1998, 37, 33–40.
   PubMed Web of Science ®Google Scholar
• Baldwin, R.L. How Hofmeister ion interactions affect protein stability. Biophysical Journal 1996, 71, 2056–2063.
   PubMed Web of Science ®Google Scholar
• Tu, A.T. Spectroscopy of biological systems. In: Advances in Spectroscopy; Clark, R.J.H.; Hester, R.E.; Eds.; Wiley: New York, 1986; 65–116.
   Google Scholar
• Li-Chan, E.C.Y. The applications of Raman spectroscopy in food science. Trends in Food Science & Technology 1996, 7, 361–370.
   Web of Science ®Google Scholar
• Maiti, N.C.; Apetri, M.M.; Zagorski, M.G.; Carey, P.R.; Anderson, V.E. Raman spectroscopic characterization of secondary structure in natively unfolded proteins: α-Synuclein. Journal of the American Oil Chemists’ Society 2004, 126, 2399–2408.
   Web of Science ®Google Scholar
• Militello, V.; Vetri, V.; Leone, M. Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophysical Chemistry 2003, 105, 133–141.
   PubMed Web of Science ®Google Scholar
• Lord, R. C. Strategy and tactics in the Raman spectroscopy of biomolecules. Applied Spectroscopy 1977, 31, 187–194.
   Web of Science ®Google Scholar