Heat-denaturation and aggregation of quinoa (Chenopodium quinoa) globulins as affected by the pH value

Food Chemistry

Volumn 196, Issue , 2016, Pages 17-24

  Mäkinen, Outi E ^a   Zannini, Emanuele ^a   Koehler, Peter ^b   Arendt, Elke K ^a  

^a UNIVERSITY COLLEGE CORK   (Ireland)

^b DEUTSCHE FORSCHUNGSANSTALT FÜR LEBENSMITTELCHEMIE   (Germany)

Author keywords

Alkali treatment; Chenopodin; Circular dichroism; Molten globule

Indexed keywords

AGGREGATES; COVALENT BONDS; DICHROISM; SOLUBILITY;

ALKALI TREATMENT; CHENOPODIN; INSOLUBLE AGGREGATES; MOLTEN GLOBULE; REDUCING CONDITIONS; RELATIVE MOLECULAR MASS; SECONDARY STRUCTURES; TERTIARY STRUCTURES;

HEATING;

GLOBULIN;

ARTICLE; CHEMICAL STRUCTURE; CHENOPODIUM QUINOA; CONTROLLED STUDY; DENATURATION; DISSOCIATION; DISULFIDE BOND; GEL; HEAT; HEATING; HYDROPHOBICITY; MOLECULAR WEIGHT; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN SECONDARY STRUCTURE; PROTEIN UNFOLDING; SOLUBILITY; CHEMISTRY; CIRCULAR DICHROISM; PROTEIN DENATURATION;

CHENOPODIUM QUINOA; CIRCULAR DICHROISM; GLOBULINS; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY;

EID: 84942036603     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.08.069     Document Type: Article

References (37)

1. L.E. Abugoch James Quinoa (Chenopodium quinoa Willd.): Composition, chemistry, nutritional, and functional properties Advances in Food and Nutrition Research 58 2009 1 31 10.1016/S1043-4526(09)58001-1
2. H. Aiking Future protein supply Trends in Food Science & Technology 22 2-3 2011 112 120 10.1016/j.tifs.2010.04.005
3. H. Ando, Y.-C. Chen, H. Tang, M. Shimizu, K. Watanabe, and T. Mitsunaga Food components in fractions of quinoa seed Food Science and Technology Research 8 1 2002 80 84 10.3136/fstr.8.80
4. C. Brinegar, and S. Goundan Isolation and characterization of chenopodin, the 11S seed storage protein of quinoa (Chenopodium quinoa) Journal of Agricultural and Food Chemistry 41 1993
5. R. Casey Distribution and some properties of seed globulins Shewry Seed proteins 1999 Springer Netherlands 159 169
6. Creighton, T. E. (Ed.). (1993). Proteins in solution and in membranes. In Proteins: Structures and molecular properties (2nd ed., pp. 261-325). New York: W.H. Freeman and Company.
7. L. Day Proteins from land plants - Potential resources for human nutrition and food security Trends in Food Science & Technology 32 1 2013 25 42 10.1016/j.tifs.2013.05.005
8. D. Elgeti, S.D. Nordlohne, M. Föste, M. Besl, M.H. Linden, V. Heinz, and T. Becker Volume and texture improvement of gluten-free bread using quinoa white flour Journal of Cereal Science 59 1 2014 41 47
9. M. Friedman Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins Journal of Agricultural and Food Chemistry 47 4 1999 1295 1319 10.1021/jf981000+
10. B. German, S. Damodaran, and J.E. Kinsella Thermal dissociation and association behavior of soy proteins Journal of Agricultural and Food Chemistry 30 5 1982 807 811 10.1021/jf00113a002
11. A. Handa, K. Takahashi, N. Kuroda, and G.W. Froning Heat-induced egg white gels as affected by pH Journal of Food Science 63 3 1998 403 407 10.1111/j.1365-2621.1998.tb15752.x
12. S. Hayakawa, and S. Nakai Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins Journal of Food Science 50 2 1985 486 491 10.1111/j.1365-2621.1985.tb13433.x
13. A.-M. Hermansson Aggregation and denaturation involved in gel formation - Chapter 5 A. Pour-El, Functionality and protein structure 1979 American Chemical Society Washington, DC 81 103
14. M. Hirose Molten globule state of food proteins Trends in Food Science & Technology 4 2 1993 48 51 10.1016/0924-2244(93)90059-J
15. H. Hu, X. Fan, Z. Zhou, X. Xu, G. Fan, and L. Wang L. Zhu Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments Ultrasonics Sonochemistry 20 1 2013 187 195 10.1016/j.ultsonch.2012.07.011
16. K.S. Kim, S. Kim, H.J. Yang, and D.Y. Kwon Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism International Journal of Food Science and Technology 39 4 2004 385 393 10.1111/j.1365-2621.2004.00795.x
17. J.E. Kinsella Relationships between structure and functional properties of food proteins P.F. Fox, J.J. Condon, Food proteins 1 1982 Applied Science Publishers Ltd. Barking, UK 51 103
18. J.E. Kinsella, D.J. Rector, and L.G. Phillips Physicochemical properties of proteins: Texturization via gelation, glass and film formation R.Y. Yada, R.L. Jackman, J.L. Smith, Protein structure-function relationships in foods 1994 Springer Boston, MA, USA 1 21 10.1007/978-1-4615-2670-4
19. O.E. Mäkinen, A.-S. Hager, and E.K. Arendt Localisation and development of proteolytic activities in quinoa (Chenopodium quinoa) seeds during germination and early seedling establishment Journal of Cereal Science 60 3 2014 484 489
20. O.E. Mäkinen, E. Zannini, and E.K. Arendt Modifying the cold gelation properties of quinoa protein isolate: Influence of heat-denaturation pH in the alkaline range Plant Foods for Human Nutrition 2015 10.1007/s11130-015-0487-4
21. M.F. Marcone Biochemical and biophysical properties of plant storage proteins Food Research International 32 2 1999 79 92 10.1016/S0963-9969(99)00061-7
22. M.F. Marcone, Y. Kakuda, and R.Y. Yada Salt-soluble seed globulins of dicotyledonous and monocotyledonous plants II. Structural characterization Food Chemistry 63 2 1998 265 274 10.1016/S0308-8146(97)00159-3
23. M.F. Marcone, R.Y. Yada, and Y. Kakuda Evidence for a molten globule state in an oligomeric plant protein Food Chemistry 60 4 1997 623 631 10.1016/S0308-8146(97)00043-5
24. S. Petruccelli, and M.C. Añón pH-induced modifications in the thermal stability of soybean protein isolates Journal of Agricultural and Food Chemistry 44 10 1996 3005 3009 10.1021/jf9600061
25. S. Prabakaran, and S. Damodaran Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation Journal of Agricultural and Food Chemistry 45 11 1997 4303 4308 10.1021/jf970269a
26. I. Prego, S. Maldonado, and M. Otegui Seed structure and localization of reserves in Chenopodium quinoa Annals of Botany 1998 481 488
27. S.W. Provencher, and J. Gloeckner Estimation of globular protein secondary structure from circular dichroism Biochemistry 20 1 1981 33 37 10.1021/bi00504a006
28. G.S. Ranhotra, J.A. Gelroth, B.K. Glaser, K.J. Lorenz, and D.L. Johnson Composition and protein nutritional quality of quinoa Cereal Chemistry 70 3 1992 303 305
29. M. Rayner, A. Timgren, M. Sjöö, and P. Dejmek Quinoa starch granules: A candidate for stabilising food-grade Pickering emulsions Journal of the Science of Food and Agriculture 92 9 2012 1841 1847 10.1002/jsfa.5610
30. J.M. Renkema, C.M. Lakemond, H.H. de Jongh, H. Gruppen, and T. van Vliet The effect of pH on heat denaturation and gel forming properties of soy proteins Journal of Biotechnology 79 3 2000 223 230 10.1016/S0168-1656(00)00239-X
31. I. Rombouts, B. Lagrain, K. Brijs, and J.A. Delcour β-Elimination reactions and formation of covalent cross-links in gliadin during heating at alkaline pH Journal of Cereal Science 52 3 2010 362 367 10.1016/j.jcs.2010.06.006
32. F. Tani, M. Murata, T. Higasa, M. Goto, N. Kitabatake, and E. Doi Molten globule state of protein molecules in heat-induced transparent food gels Journal of Agricultural and Food Chemistry 43 9 1995 2325 2331 10.1021/jf00057a003
33. S. Utsumi, S. Damodaran, and J.E. Kinsella Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and beta subunits of 7S Journal of Agricultural and Food Chemistry 32 6 1984 1406 1412 10.1021/jf00126a047
34. R.W. Visschers, and H.H.J. de Jongh Disulphide bond formation in food protein aggregation and gelation Biotechnology Advances 23 1 2005 75 80 10.1016/j.biotechadv.2004.09.005
35. D.B. Volkin, H. Mach, and C.R. Middaugh Degradative covalent reactions important to protein stability Molecular Biotechnology 8 2 1997 105 122
36. R. Westermeier Sensitive, quantitative, and fast modifications for Coomassie Blue staining of polyacrylamide gels Proteomics 6 S2 2006 61 64 10.1002/pmic.200690121
37. J.R. Whitaker, and R.E. Feeney Chemical and physical modification of proteins by the hydroxide ion Critical Reviews in Food Science and Nutrition 19 3 1983 173 212 10.1080/10408398309527375