Effect of acid treatment on structural and foaming properties of soy amaranth protein mixtures

Food Hydrocolloids

Volumn 29, Issue 2, 2012, Pages 272-279

  Ventureira, J L ^a   Martinez E N ^a   Anon M C ^a  

^a CENTRO DE INVESTIGACIÓN Y DESARROLLO EN CRIOTECNOLOGÍA DE ALIMENTOS CIDCA   (Argentina)

Author keywords

Acid neutralization treatment; Amaranth protein; Foaming properties; Soy proteins

Indexed keywords

AMARANTHUS CAUDATUS; GLYCINE MAX;

EID: 84860562490     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2012.03.013     Document Type: Article

References (38)

1. Abugoch L., Martínez E.N., Añón M.C. Influence of pH on structure and function of amaranth (Amaranthus hypochondriacus) protein isolates. Cereal Chemistry 2010.
2. Avanza M.V., Puppo M.C., Añón M.C. Rheological characterization of amaranth protein gels. Food Hydrocolloids 2005, 19:889-898.
3. Becker R., Wheeler E.L., Lorenz K., Stafford A.E., Grosjean O.K., Betschart A.A., et al. A compositional study of amaranth grain. Journal of Food Science 1981, 46:1175-1180.
4. Bejarano-Luján D.L., Lopes da Cunha R., Netto F.M. Structural and rheological properties of amaranth protein concentrate gels obtained by different processes. Food Hydrocolloids 2010, 24:602-610.
5. Bressani R. Composition and nutritional properties of amaranth. Amaranth. Biology, chemistry and technology 1994, 185-205. CRC Press, Boca Raton. O. Paredes-López (Ed.).
6. Cardamone M., Puri N.K. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochemical Journal 1992, 282:589-593.
7. Condes M., Scilingo A., Añón M.C. Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes. LWT - Food Science and Technology 2009, 42:963-970.
8. Damodaran S. Structure-function relationship of food proteins. Protein functionality in food systems 1994, 1-38. Marcel Dekker, New York. N.S. Hettiarachchy, G.R. Z (Eds.).
9. Damodaran S. Protein-stabilized foams and emulsions. Food proteins and their applications 1997, 57-107. Marcel Dekker, New York. S. Damodaran, A. Paraf (Eds.).
10. Fidantsi A., Doxastakis G. Emulsifying and foaming properties of amaranth seed protein isolates. Colloids and Surfaces B: Biointerfaces 2001, 21:119-124.
11. Graham D.E., Phillips M.C. The conformation of proteins at the air water interface and their role in stabilizing foams. Foams 1976, 237-255. Academic Press, New York. R.J. Akers (Ed.).
12. Guillotea M., Lalo L., Michaux S., Bucheli P., McCarthy J. Identification and characterization of the major aspartic proteinase activity in Theobroma cacao seeds. Journal of the Science, Food and Agriculture 2005, 85:549-562.
13. Hettiarachchy N.S., Kalapathy U. Functional properties of soy proteins. Functional properties of proteins and lipids 1998, 80-95. American Chemical Society, Washington, DC. J.R. Whitaker, S. Fereidoon, A.L. Munguia, R.Y. Yada, G. Fuller (Eds.).
14. Jiang J., Chen J., Xiong Y.L. Structural and emulsifying properties of soy proteins isolate subjected to acid and alkaline pH-shifting processes. Journal of Agricultural and Food Chemistry 2009, 57:7576-7583.
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-684.
16. Liu K. Expanding soybean food utilization. Food Technology 2000, 54:46-59.
17. Loisel W.G.J., Gueguen J., Popineau Y. A new apparatus for analyzing foaming properties of proteins. Food proteins: Structure and functionality 1993, 320-323. VCH, Weinheim, Germany. K.D. Schwenke, R. Mothes (Eds.).
18. Mahajan A., Dua S. Salts and pH induced changes in functional properties of amaranth (Amaranthus tricolor L.) seed meal. Cereal Chemistry 2002, 79:834-837.
19. Marcone M.F., Kakuda Y. A comparative study of the functional properties of amaranth and soybean globulin isolate. Nahrung 1999, 43:368-373.
20. Martínez S.N., Añón M.C. Composition and structural characterization of amaranth protein isolates. An electrophoretic and calorimetric study. Journal of Agricultural and Food Chemistry 1996, 44:2523-2530.
21. Molina Ortiz S.E., Wagner J.R. Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties. Food Research International 2002, 35:511-518.
22. Mutlu A., Chen X., Reddy S.M., Gal S. The aspartic proteinase is expressed in Arabidopsis thaliana seeds and localized in the protein bodies. Seed Science Research 1999, 9:75-84.
23. Permyakov E.A. Protein luminiscence. Luminiscent spectroscopy of proteins 1993, 57-79. CRC Press, Boca Raton.
24. Petruccelli S., Añón M.C. Relationship between the method of obtention and the structural and functional properties of soy protein isolates. 1. Structural and hydration properties. Journal of Agricultural and Food Chemistry 1994, 42:2161-2169.
25. Ruíz-Henestrosa V.P., Sánchez C.C., Pedroche J.J., Millán F., Rodríguez Patino J.M. Improving the functional properties of soy glycinin by enzymatic treatment. Adsorption and foaming characteristics. Food Hydrocolloids 2009, 23:377-386.
26. Runeberg-Roos P., Tormakangas K., Ostman A. Primary structure of a barley-grain aspartic proteinase. European Journal of Biochemistry 1991, 202:1021-1027.
27. Scilingo A., Molina Ortiz S., Martinez E.N., Añón M.C. Amaranth protein isolates modified by hydrolytic and thermal treatments. Relationship between structure and solubility. Food Research International 2002, 35:855-862.
28. Tormakangas K., Kervinen J., Ostman A., Teeri T. Tissue specific localization of aspartic proteinase in developing and germinating barley grains. Planta 1994, 195,116-125.
29. Utsumi S., Matsumura Y., Mori T. Structure-function relationships of soy proteins. Food proteins and their applications 1997, 257-292. Dekker, New York. S. Damodaran, A. Paraf (Eds.).
30. Ventureira J., Martínez E.N., Añón M.C. Stability of oil: water emulsions of amaranth proteins. Effect of hydrolysis and pH. Food Hydrocolloids 2010, 24:551-559.
31. Wagner J.R., Gueguen J. Surface functional properties of native, acid-treated, and reduced soy glycinin. 1. Foaming properties. Journal of Agricultural and Food Chemistry 1999, 47:2173-2180.
32. 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.
33. Walstra P. Principles of foam formation and stability. Foam: Physics, chemistry and structure 1989, Springer-Verlag, London. A.J. Wilson (Ed.).
34. Ward A.F.H., Tordai L. Time-dependence of boundary tensions of solutions 1. The role of diffusion in time-effects. The Journal of Chemical Physics 1946, 14:453-461.
35. Wilson A.L. Soy foods. Practical handbook of soybean processing and utilization 1995, 428-459. American Soybean Association/American Oil Chemist's Society, St. Louis, MO/Champaign, IL. D.R. Erickson (Ed.).
36. Xu S., Damodaran S. Kinetics of adsorption of proteins at the air-water interface from a binary mixture. Langmuir 1994, 10:472-480.
37. Yalçin E., Çelik S. Solubility properties of barley flour, protein isolates and hydrolysates. Food Chemistry 2007, 104:1641-1647.
38. Zayas J.F. Functionality of proteins in food 1997, Springer-Verlag, Berlin Heidelberg.