Determination of heat-set gelation capacity of a quinoa protein isolate (Chenopodium quinoa) by dynamic oscillatory rheological analysis

Food Chemistry

Volumn 232, Issue , 2017, Pages 263-271

  Kaspchak, Elaine ^a   Oliveira, Marco Aurelio Schüler de ^b   Simas, Fernanda Fogagnoli ^a   Franco, Célia Regina Cavicchiolo ^a   Silveira, Joana Léa Meira ^a   Mafra, Marcos Rogério ^a   Igarashi Mafra, Luciana ^a  

^a FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

^b STATE UNIVERSITY OF MARINGÁ   (Brazil)

Author keywords

11S globulin; Divalent ions; Heat set gelation; Microstructure; Rheology

Indexed keywords

ELECTROPHORESIS; GELATION; GELS; MASS SPECTROMETRY; MICROSTRUCTURE; RHEOLOGY;

11S GLOBULIN; DIVALENT IONS; MASS SPECTROMETRY ANALYSIS; PROTEIN ISOLATES; PROTEIN SURFACE; QUINOA PROTEINS; RHEOLOGICAL ANALYSIS; SECONDARY STRUCTURES;

PROTEINS;

CALCIUM CHLORIDE; GLOBULIN; INORGANIC SALT; MAGNESIUM CHLORIDE; PLANT PROTEIN; GEL;

ARTICLE; CHENOPODIUM QUINOA; CIRCULAR DICHROISM; ELECTROPHORESIS; FLOW KINETICS; GELATION; HEAT SET GELATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; OSCILLATION; PH; PROTEIN ISOLATION; PROTEIN SECONDARY STRUCTURE; SCANNING ELECTRON MICROSCOPY; SOLUBILITY; SURFACE CHARGE; VISCOELASTICITY; CHEMISTRY; GEL; HEAT; ISOLATION AND PURIFICATION;

CHENOPODIUM QUINOA; GELS; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; PLANT PROTEINS; RHEOLOGY;

EID: 85017258504     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.04.014     Document Type: Article

References (37)

1. Abugoch, L.E., Romero, N., Tapia, C.A., Silva, J., Rivera, M., Study of some physicochemical and functional properties of quinoa (Chenopodium quinoa Willd) protein isolates. Journal of Agricultural and Food Chemistry 56 (2008), 4745–4750, 10.1021/jf703689u.
2. Ako, K., Nicolai, T., Durand, D., Salt-induced gelation of globular protein aggregates: Structure and kinetics. Biomacromolecules 11:4 (2010), 864–871, 10.1021/bm9011437.
3. Ando, H., Chen, Y., Tang, H., Shimizu, M., Watanabe, K., Mitsunaga, T., Food components in fractions of quinoa seed. Food Science and Technology Research 8:1 (2002), 80–84, 10.3136/fstr.8.80.
4. AOAC, Official methods of analysis of AOAC international. 13th ed., 2008, AOAC International, Gaithersburg.
5. Avanza, M.V., Puppo, M.C., Añón, M.C., Rheological characterization of amaranth protein gels. Food Hydrocolloids 19:5 (2005), 889–898, 10.1016/j.foodhyd.2004.12.002.
6. Baier, S.K., McClements, D.J., Influence of cosolvent systems on the gelation mechanism of globular protein thermodynamic, kinetic, and structural aspects of globular protein gelation. Comprehensive Reviews in Food Science and Food Safety 4 (2005), 43–54, 10.1016/j.foodhyd.2004.12.002.
7. Bejarano-Luján, D.L., Cunha, R.L., Netto, F.M., Structural and rheological properties of amaranth protein concentrate gels obtained by different processes. Food Hydrocolloids 24:6–7 (2010), 602–610, 10.1016/j.foodhyd.2010.02.007.
8. Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye binding. Analytical Biochemistry 72 (1976), 248–254, 10.1016/0003-2697(76)90527-3.
9. Brinegar, C., Goundan, S., Isolation and characterization of chenopodin, the 11S seed storage protein of quinoa (Chenopodium quinoa). Journal of Agricultural and Food Chemistry 41:2 (1993), 182–185, 10.1021/jf00026a006.
10. 2 on cold-set gelation of heat-denatured whey protein. Journal of Food Science 65:5 (2000), 801–804, 10.1111/j.1365-2621.2000.tb13590.x.
11. Canabady-Rochelle, L.S., Sanchez, C., Mellema, M., Banon, S., Calcium carbonate-hydrolyzed soy protein complexation in the presence of citric acid. Journal of Colloid and Interface Science 345:1 (2010), 88–95, 10.1016/j.jcis.2010.01.037.
12. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F., Colorimetric method for determination of sugars and related substances. Analytical Chemistry 28:3 (1956), 350–356, 10.1021/ac60111a017.
13. Elsohaimy, S.A., Refaay, T.M., Zaytoun, M.A.M., Physicochemical and functional properties of quinoa protein isolate. Annals of Agricultural Sciences 60:2 (2015), 297–305, 10.1016/j.aoas.2015.10.007.
14. Foegeding, E.A., Food biophysics of protein gels: A challenge of nano and macroscopic proportions. Food Biophysics 1:1 (2006), 41–50, 10.1007/s11483-005-9003-y.
15. Foegeding, E.A., Rheology and sensory texture of biopolymer gels. Current Opinion in Colloid & Interface Science 12:4–5 (2007), 242–250, 10.1016/j.cocis.2007.07.001.
16. Hua, Y., Cui, S.W., Wang, Q., Mine, Y., Poysa, V., Heat induced gelling properties of soy protein isolates prepared from different defatted soybean flours. Food Research International 38:4 (2005), 377–385, 10.1016/j.foodres.2004.10.006.
17. Jancurová, M., Minarovičová, L., & Dandár, A. (2009). Quinoa – A review, 27(2), 71–79.
18. Kinsella, J.E., Functional properties of soy proteins. Journal of the American Oil Chemists’ Society 56:3 (1979), 242–258, 10.1007/BF02671468.
19. Koziol, M., Chemical composition and nutritional evaluation of quinoa (Chenopodium quinoa Willd.). Journal of Food Composition and Analysis 5:1 (1992), 35–68.
20. Kundu, S., Chinchalikar, A.J., Das, K., Aswal, V.K., Kohlbrecher, J., Mono-, di- and tri-valent ion induced protein gelation: Small-angle neutron scattering study. Chemical Physics Letters 593 (2014), 140–144, 10.1016/j.cplett.2013.12.068.
21. Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:5259 (1970), 680–685, 10.1038/227680a0.
22. Lakemond, C.M.M., Jongh, H.H.J., Paques, M., Vlieta, T., Gruppena, H., Voragena, A.G.J., Gelation of soy glycinin; influence of pH and ionic strength on network structure in relation to protein conformation. Food Hydrocolloids 17:3 (2003), 365–377, 10.1016/S0268-005X(02)00100-5.
23. Lu, X., Lu, Z., Yin, L., Cheng, Y., Li, L., Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel. Food Research International 43:6 (2010), 1673–1683, 10.1016/j.foodres.2010.05.011.
24. ++ na dureza de géis de concentrado proteico de soro bovino. Ciência E Tecnologia de Alimentos 22:2 (2002), 205–209.
25. Mäkinen, O.E., Zannini, E., Arendt, E.K., Modifying the cold gelation properties of quinoa protein isolate: Influence of heat-denaturation pH in the alkaline range. Plant Foods for Human Nutrition 70 (2015), 250–256, 10.1007/s11130-015-0487-4.
26. Mäkinen, O.E., Zannini, E., Koehler, P., Arendt, E.K., Heat-denaturation and aggregation of quinoa (Chenopodium quinoa) globulins as affected by the pH value. Food Chemistry 196 (2016), 17–24, 10.1016/j.foodchem.2015.08.069.
27. Matiacevich, S.B., Castellión, M.L., Maldonado, S.B., Buera, M.P., Water-dependent thermal transitions in quinoa embryos. Thermochimica Acta 448:2 (2006), 117–122, 10.1016/j.tca.2006.06.016.
28. Nayak, P., Sahoo, S.K., Behera, A., Nanda, P.K., Nayak, P.L., Guru, B.C., Synthesis and characterization of soy protein isolate/MMT nanocomposite film for the control release of the drug ofloxacin. World Journal of Nano Science and Engineering 01 (2011), 27–36, 10.4236/wjnse.2011.12005.
29. Ramos, Ó.L., Pereira, J.O., Silva, S.I., Amorim, M.M., Fernandes, J.C., Lopes-da-Silva, J.A., et al. Effect of composition of commercial whey protein preparations upon gelation at various pH values. Food Research International 48:2 (2012), 681–689, 10.1016/j.foodres.2012.06.004.
30. Renkema, J.M.S., Lakemond, C.M.M., De Jongh, H.H.J., Gruppen, H., Van Vliet, T., The effect of pH on heat denaturation and gel forming properties of soy proteins. Journal of Biotechnology 79 (2000), 223–230, 10.1016/S0168-1656(00)00239-X.
31. Renkema, J.M.S., Van Vliet, T., Heat-induced gel formation by soy proteins at neutral pH. Journal of Agricultural and Food Chemistry 50 (2002), 1569–1573, 10.1021/jf010763l.
32. Ruales, J., Nair, B.M., Nutritional quality of the protein in quinoa (Chenopodium quinoa, Willd) seeds. Plant Foods for Human Nutrition 42:1 (1992), 1–11, 10.1007/BF02196067.
33. Ruiz, G.A., Xiao, W., Van Boekel, M., Minor, M., Stieger, M., Effect of extraction pH on heat-induced aggregation, gelation and microstructure of protein isolate from quinoa (Chenopodium quinoa Willd). Food Chemistry 209 (2016), 203–210, 10.1016/j.foodchem.2016.04.052.
34. Sreerama, N., Woody, R.W., Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Analytical Biochemistry 287:2 (2000), 252–260, 10.1006/abio.2000.4880.
35. Su, Y., Dong, Y., Niu, F., Wang, C., Liu, Y., Yang, Y., Study on the gel properties and secondary structure of soybean protein isolate/egg white composite gels. European Food Research and Technology 240:2 (2015), 367–378, 10.1007/s00217-014-2336-3.
36. Tarone, A.G., Fasolin, L.H., Perrechil, F.D.A., Hubinger, M.D., Cunha, R.L. Da., Influence of drying conditions on the gelling properties of the 7S and 11S soy protein fractions. Food and Bioproducts Processing 91:2 (2013), 111–120, 10.1016/j.fbp.2012.11.010.
37. Toapanta, A., Carpio, C., Vilcacundo, R., Carrillo, W., Analysis of protein isolate from quinoa (Chenopodium Quinoa Willd). Asian Journal of Pharmaceutical and Clinical Research 9:2 (2016), 11–12.