Effect of Maillard reaction conditions on the degree of glycation and functional properties of whey protein isolate - Maltodextrin conjugates

Food Hydrocolloids

Volumn 38, Issue , 2014, Pages 110-118

  Garcia Amezquita, L E ^a   Martinez Alvarenga, M S ^a   Olivas, G I ^a   Zamudio Flores, P B ^a   Acosta Muniz C H ^a   Sepulveda, D R ^a  

^a CENTRO DE INVESTIGACIÓN EN ALIMENTACIÓN Y DESARROLLO   (Mexico)

Author keywords

Functional properties; Maillard reaction; Maltodextrin; Whey protein isolate

Indexed keywords

CHEMICAL REACTIONS; COLOR; COLORIMETRY; ELECTROPHORESIS; GLYCOSYLATION; POLYSACCHARIDES; PROTEINS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

AMINO GROUP; COLOR CHANGES; FUNCTIONAL PROPERTIES; GLYCATION; MAILLARD REACTION; MALTODEXTRINS; PROTEIN FUNCTIONALITIES; REACTION CONDITIONS; WATER ACTIVITY; WHEY PROTEIN ISOLATE;

SOLUBILITY;

EID: 84890810228     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2013.11.006     Document Type: Article

References (57)

1. Achouri A., Boye J.I., Yaylayan V.A., Yeboah F.K. Functional properties of glycated soy 11S glycinin. Journal of Food Science 2005, 70:269-274.
2. Akhtar M., Dickinson E. Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum arabic. Food Hydrocolloids 2007, 21:607-616.
3. Aoki T., Hiidome Y., Kitahata K., Sugimoto Y., Ibrahim H., Kato Y. Improvement of heat stability and emulsifying activity of ovalbumin by conjugation with glucuronic acid through the Maillard reaction. Food Research International 1999, 32:129-133.
4. Bosch L., Alegría A., Farre R., Clemente G. Fluorescence and color as markers for the Maillard reaction in milk-cereal based infant foods during storage. Food Chemistry 2007, 105:1135-1143.
5. Broersen K., Voragen A.G.J., Hamer R.J., Jongh H.H.J. Glycoforms of β-lactoglobulin with improved thermostability and preserved structural packing. Biotechnology and Bioengineering 2004, 86:78-87.
6. Buera M.P., Karel M. Application of the WLF equation to describe the combined effects of moisture and temperature on nonenzymatic browning rates in food systems. Journal of Food Processing and Preservation 1993, 17:31-45.
7. Chevalier F., Chobert J.M., Dalgalarrondo M., Choiset Y., Haertlé T. Maillard glycation of β-lactoglobulin induces conformation changes. Nahrung/Food 2002, 46:58-63.
8. Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertlé T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. International Dairy Journal 2001, 11:145-152.
9. Church F.C., Swaisgood H.E., Porter D.H., Catignani G.L. Spectrophotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science 1983, 66:1219-1227.
10. Corzo-Martínez M., Moreno F.J., Olano A., Villamiel M. Structural characterization of bovine β-lactoglobulin-galactose/tagatose Maillard complexes by electrophoretic, chromatographic, and spectroscopic methods. Journal of Agricultural and Food Chemistry 2008, 56:4244-4252.
11. Corzo-Martínez M., Moreno F.J., Villamiel M., Harte F.M. Characterization and improvement of rheological properties of sodium caseinate glycated with galactose, lactose and dextran. Food Hydrocolloids 2009, 24:88-97.
12. Desrosiers T., Savoie L. Extent of damage to amino acid availability of whey protein heated with sugar. Journal of Dairy Research 1991, 58:431-441.
13. Dunlap C.A., CÔté G.L. β-lactoglobulin-dextran conjugates: effect of polysaccharide size on emulsion stability. Journal of Agricultural and Food Chemistry 2005, 53:419-423.
14. Einhorn-Stoll U., Ulbrich M., Sever S., Kunzek H. Formation of milk protein-pectin conjugates with improved emulsifying properties by controlled dry heating. Food Hydrocolloids 2005, 19:329-340.
15. Fenaille F., Morgan F., Parisod V., Tabet J.C., Guy P.A. Solid-state glycation of β-lactoglobulin monitored by electrospray ionisation mass spectrometry and gel electrophoresis techniques. Rapid Communications in Mass Spectrometry 2003, 17:1483-1492.
16. Gauthier F., Bouhallab S., Renault A. Modification of bovine β-lactoglobulin by glycation in a powdered state or in aqueous solution: adsorption at the air-water interface. Colloids and Surfaces B: Biointerfaces 2001, 21:37-45.
17. Hiller B., Lorenzen P.C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Research International 2010, 43:1155-1166.
18. Hodge J.E. Chemistry of browning reactions in model systems. Journal of Agricultural and Food Chemistry 1953, 1:928-943.
19. Jiang Z., Brodkorb A. Structure and antioxidant activity of Maillard reaction products from α-lactalbumin and β-lactoglobulin with ribose in an aqueous model system. Food Chemistry 2012, 133:960-968.
20. Jiménez-Castaño L., López-Fandiño R., Olano A., Villamiel M. Study on β-lactoglobulin glycosylation with dextran: effect on solubility and heat stability. Food Chemistry 2005, 93:689-695.
21. Jiménez-Castaño L., Villamiel M., López-Fandiño R. Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocolloids 2007, 21:433-443.
22. Kato A. Industrial applications of Maillard type protein-polysaccharide conjugates. Food Science and Technology Research 2002, 8:193-199.
23. Labuza T.P., Baisier W.M. The kinetics of nonenzymatic browning. Physical chemistry of foods 1992, 281-304. Marcel Dekker, New York. H.G. Schwartzberg, R.W. Hartel (Eds.).
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
25. Lillard J.S., Clare D.A., Daubert C.R. Glycosylation and expanded utility of a modified whey protein ingredient via carbohydrate conjugation at low pH. Journal of Dairy Science 2009, 92:35-48.
26. Li Y., Lu F., Luo C., Chen Z., Mao J., Shoemaker C., et al. Functional properties of the Maillard reaction products of rice protein with sugar. Food Chemistry 2009, 117:69-74.
27. Liu P., Huang M., Song S., Hayat K., Zhang X., Xia S., et al. Sensory characteristics and antioxidant activities of Maillard reaction products from soy protein hydrolysates with different molecular weight distribution. Food and Bioprocess Technology 2012, 5:1775-1789.
28. Malec L.S., Pereyra Gonzales A.S., Naranjo G.B., Vigo M.S. Influence of water activity and storage temperature on lysine availability of a milk like system. Food Research International 2002, 35:849-853.
29. Matiacevich S.B., Buera M.P. Acritical evaluation of fluorescenceas a potential marker for the Maillard reaction. Food Chemistry 2006, 95:423-430.
30. Medrano A., Abirached C., Panizzolo L., Moyna P., Añón M.C. The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chemistry 2009, 113:127-133.
31. Mesa M.D., Silván J.M., Olza J., Gil A., Castillo M.D. Antioxidant properties of soy protein-fructooligosaccharide glycation systems and its hydrolyzates. Food Research International 2008, 41:606-615.
32. Mine Y., Yang M. Functional properties of egg components in food systems. Handbook of poultry science and technology 2010, 579-630. John Wiley and Sons, Inc, New Jersey. I. Guerrero-Legarreta (Ed.).
33. Miralles B., Martínez-Rodríguez A., Santiago A., Lagemaat J.D., Heras A. The occurrence of a Maillard-type protein-polysaccharide reaction between β-lactoglobulin and chitosan. Food Chemistry 2007, 100:1071-1075.
34. Morgan F., Leonil J., Mollé D., Bouhallab S. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. Journal of Agricultural and Food Chemistry 1999, 47:83-91.
35. Morgan F., Mollé D., Henry G., Vénien A., Léonil J., Peltre G., et al. Glycation of bovine β-lactoglobulin: effect on the protein structure. International Journal of Food Science and Technology 1999, 34:429-435.
36. Morris G.A., Sims I.M., Robertson A.J., Furneaux R.H. Investigation into the physical and chemical properties of sodium caseinate-maltodextrin glyco-conjugates. Food Hydrocolloids 2004, 18:1007-1014.
37. Nacka F., Chobert J.M., Burova T., Leonil J., Haertlé T. Induction of new physicochemical and functional properties by the glycosylation of whey proteins. Journal of Protein Chemistry 1998, 17:495-503.
38. Nakamura S., Kato A., Kobayashi K. Bifunctional lysozyme-galactomannan conjugate having excellent emulsifying properties and bactericidal effect. Journal of Agricultural and Food Chemistry 1992, 40:735-739.
39. Oliver C.M., Melton L.D., Stanley R.A. Creating proteins with novel functionality via the Maillard reaction: a review. Critical Reviews in Food Science and Nutrition 2006, 46:337-350.
40. Oliver C.M., Melton L.D., Stanley R.A. Glycation of caseinate by fructose and fructooligosaccharides during controlled heat treatment in the 'dry' state. Journal of the Science of Food and Agriculture 2006, 86:722-731.
41. O'Regan J., Mulvihill D.M. Preparation, characterisation and selected functional properties of sodium caseinate-maltodextrin conjugates. Food Chemistry 2009, 115:1257-1267.
42. Pagliarini E., Peri C., Abba S. Kinetics study on colour changes in milk due to heat. Journal of Food Science 1990, 55:1766-1767.
43. Pan G.G., Melton L.D. Nonenzymatic browning of lactose and caseinate during dry heating at different relative humidities. Journal of Agricultural and Food Chemistry 2007, 55:10036-10042.
44. Phillips L.G., German J.B., O'neill T.E., Foegeding E.A., Harwalkar V.R., Kilara A., et al. Standardized procedure for measuring foaming properties of three proteins, a collaborative study. Journal of Food Science 1990, 55:1441-1453.
45. Phillips L.G., Schulman W., Kinsella J.E. pH and heat treatment effects on foaming of whey protein isolate. Journal of Food Science 1990, 55:1116-1119.
46. Renn P.T., Sathe S.K. Effects of pH, temperature, and reactant molar ratio on l-leucine and d-glucose Maillard browning reaction in an aqueous system. Journal of Agricultural and Food Chemistry 1997, 45:3782-3787.
47. Rozycki S.D., Buera M.P., Piagentini A.M., Costa S.C., Pauletti M.S. Advances in the study of the kinetics of color and fluorescence development in concentrated milk systems. Journal of Food Engineering 2010, 101:59-66.
48. Scaman C., Nakai S., Aminlari M. Effect of pH, temperature and sodium bisulfite or cysteine on the level of Maillard-based conjugation of lysozyme with dextran, galactomannan and mannan. Food Chemistry 2006, 99:368-380.
49. Shepherd R., Robertson A., Ofman D. Dairy glycoconjugate emulsifiers: casein-maltodextrins. Food Hydrocolloids 2000, 14:281-286.
50. Sun Y., Hayakawa S., Izumori K. Modification of ovalbumin with a rare ketohexose through the Maillard reaction: effect on protein structure and gel properties. Journal of Agricultural and Food Chemistry 2004, 52:1293-1299.
51. Tunick M.H. Whey protein production and utilization: a brief study. Whey processing, functionality and health benefits 2008, 1-14. John Wiley and Sons, Inc, Iowa. C.I. Onwulata, P.J. Huth (Eds.).
52. Walstra P., Wouters J.T.M., Geurts T.J. Dairy science and technology 2006, CRC Press, Boca Raton. 2nd ed.
53. Wooster T.J., Augustin M.A. Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocolloids 2007, 21:1072-1080.
54. Wooster T.J., Augustin M.A. The emulsion flocculation stability of protein-carbohydrate diblock copolymers. Journal of Colloid and Interface Science 2007, 313:665-675.
55. Yeboah F.K., Alli I., Yaylayan V.A., Konishi Y., Stefanowicz P. Monitoring glycation of lysozyme by electrospray ionization mass spectrometry. Journal of Agricultural and Food Chemistry 2000, 48:2766-2774.
56. Zeng Y., Zhang X., Guan Y., Sun Y. Characteristics and antioxidant activity of Maillard reaction products from psicose-lysine and fructose-lysine model systems. Journal of Food Science 2011, 56:C398-C403.
57. Zhu D., Damodaran S., Lucey J.A. Formation of whey protein isolate-dextran conjugates in in aqueous solutions. Journal of Agricultural and Food Chemistry 2008, 56:7113-7118.