Effect of hydrogen peroxide on improving the heat stability of whey protein isolate solutions

Food Chemistry

Volumn 223, Issue , 2017, Pages 114-120

  Sutariya, Suresh ^a   Patel, Hasmukh ^a,b  

^a SOUTH DAKOTA STATE UNIVERSITY   (United States)

^b Land O'Lakes Animal Milk Products   (United States)

Author keywords

Gelation; Heat stability; Hydrogen peroxide; Whey protein; Lactoglobulin

Indexed keywords

DEIONIZED WATER; DENATURATION; GELATION; HEAT TREATMENT; HYDROGEN PEROXIDE; OXIDATION; PEROXIDES; STABILITY;

AFTER-HEAT TREATMENT; BETA-LACTOGLOBULIN; HEAT STABILITY; INTERCHANGE REACTIONS; LACTOGLOBULIN; RHEOLOGICAL PROPERTY; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

PROTEINS;

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; HYDROGEN PEROXIDE; THIOL DERIVATIVE; WHEY PROTEIN; LACTALBUMIN; LACTOGLOBULIN; MILK PROTEIN; SOLUTION AND SOLUBILITY;

ARTICLE; CELL METABOLISM; CONTROLLED STUDY; ENVIRONMENTAL PARAMETERS; GELATION; HEAT COAGULATION TIME TEST; HEAT TREATMENT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN AGGREGATION; PROTEIN CONTENT; PROTEIN DENATURATION; SOLUTION AND SOLUBILITY; THERMOSTABILITY; ADVERSE EFFECTS; ANALYSIS; DRUG EFFECTS; FLOW KINETICS; HEAT; METABOLISM; PH; PROCEDURES; PROTEIN STABILITY;

HOT TEMPERATURE; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; LACTOGLOBULINS; MILK PROTEINS; PROTEIN DENATURATION; PROTEIN STABILITY; RHEOLOGY; SOLUTIONS; WHEY PROTEINS;

EID: 85006892686     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.12.013     Document Type: Article

References (41)

1. 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 4:3 (2005), 43–54.
2. CFR, 21CFR184.1366: Listing of specific substances affirmed as GRAS: Hydrogen peroxide. Code of Federal Regulations, vol. 3, 2014, Silver Spring, MD 20993.
3. Cho, Y., Gu, W., Wakins, S., Lee, S.-P., Kim, T.-R., Brady, J.W., Batt, C.A., Thermostable variants of bovine β-lactoglobulin. Protein Engineering 7:2 (1994), 263–283.
4. Considine, T., Patel, H., Anema, S., Singh, H., Creamer, L., Interactions of milk proteins during heat and high hydrostatic pressure treatments—A review. Innovative Food Science & Emerging Technologies 8:1 (2007), 1–23.
5. Considine, T., Patel, H.A., Singh, H., Creamer, L.K., Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of beta-lactoglobulin B. Journal of Agricultural and Food Chemistry 53:8 (2005), 3197–3205.
6. Considine, T., Patel, H.A., Singh, H., Creamer, L.K., Influence of binding conjugated linoleic acid and myristic acid on the heat-and high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Food Chemistry 102:4 (2007), 1270–1280.
7. Considine, T., Singh, H., Patel, H.A., Creamer, L.K., Influence of binding of sodium dodecyl sulfate, All-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Journal of Agricultural and Food Chemistry 53:20 (2005), 8010–8018.
8. Conte, M., Carroll, K., The chemistry of thiol oxidation and detection. Jakob, U., Reichmann, D., (eds.) Oxidative stress and redox regulation, 2013, Springer, Netherlands, 1–42.
9. Creamer, L.K., Bienvenue, A., Nilsson, H., Paulsson, M., van Wanroij, M., Lowe, E.K.,.. Jimenez-Flores, R., Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine beta-lactoglobulin. Journal of Agriculture and Food Chemistry 52:25 (2004), 7660–7668.
10. de Wit, J.N., Swinkels, G.A., A differential scanning calorimetric study of the thermal denaturation of bovine beta-lactoglobulin. Thermal behaviour at temperatures up to 100 °C. Biochimica et Biophysica Acta 624:1 (1980), 40–50.
11. Dissanayake, M., Vasiljevic, T., Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science 92:4 (2009), 1387–1397.
12. Doucet, D., Foegeding, E.A., Gel formation of peptides produced by extensive enzymatic hydrolysis of beta-lactoglobulin. Biomacromolecules 6:2 (2005), 1140–1148.
13. Fish, N.L., Mickelsen, R., Effect of hydrogen peroxide on whey protein nitrogen value of heated skimmilk1. Journal of Dairy Science 50:7 (1967), 1045–1048.
14. Foegeding, E.A., Davis, J.P., Doucet, D., McGuffey, M.K., Advances in modifying and understanding whey protein functionality. Trends in Food Science & Technology 13:5 (2002), 151–159.
15. Gosal, W.S., Ross-Murphy, S.B., Globular protein gelation. Current Opinion in Colloid & Interface Science 5:3–4 (2000), 188–194.
16. Hirano, R., Hirano, M., Hatanaka, K., Changes in hardness of acid milk gel by addition of hypothiocyanite ion, hydrogen peroxide and their effects on sulfhydryls in milk proteins. Journal of the Japanese Society for Food Science and Technology 46:6 (1999), 376–381.
17. Huxtable, R.J., Biochemistry of sulfur. 1986, Published by Plenum Press, New York.
18. Iametti, S., De Gregori, B., Vecchio, G., Bonomi, F., Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulin. European Journal of Biochemistry 237:1 (1996), 106–112.
19. Jayat, D., Gaudin, J.C., Chobert, J.M., Burova, T.V., Holt, C., McNae, I.,.. Haertle, T., A recombinant C121S mutant of bovine beta-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating. Biochemistry 43:20 (2004), 6312–6321.
20. Kuhn, P.R., Foegeding, E.A., Factors influencing whey protein gel rheology: Dialysis and calcium chelation. Journal of Food Science 56:3 (1991), 789–791.
21. Kulmyrzaev, A., Bryant, C., McClements, D.J., Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. Journal of Agricultural and Food Chemistry 48:5 (2000), 1593–1597.
22. Lucey, J.A., Milk protein gels. Singh, A.T.B., (eds.) Milk proteins, 2008, Academic Press, San Diego, 449–481.
23. Patel, H.A., Singh, H., Havea, P., Considine, T., Creamer, L.K., Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions. Journal of Agricultural and Food Chemistry 53:24 (2005), 9590–9601.
24. Qi, X.L., Brownlow, S., Holt, C., Sellers, P., Thermal denaturation of beta-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05. Biochimica Biophysica Acta 1248:1 (1995), 43–49.
25. Reddie, K.G., Carroll, K.S., Expanding the functional diversity of proteins through cysteine oxidation. Current Opinion in Chemical Biology 12:6 (2008), 746–754.
26. Rich, L.M., Foegeding, E.A., Effects of sugars on whey protein isolate gelation. Journal of Agricultural and Food Chemistry 48:10 (2000), 5046–5052.
27. Rocha, C., Teixeira, J.A., Hilliou, L., Sampaio, P., Gonçalves, M.P., Rheological and structural characterization of gels from whey protein hydrolysates/locust bean gum mixed systems. Food Hydrocolloids 23 (2009), 1734–1745.
28. Ryan, K.N., Vardhanabhuti, B., Jaramillo, D.P., van Zanten, J.H., Coupland, J.N., Foegeding, E.A., Stability and mechanism of whey protein soluble aggregates thermally treated with salts. Food Hydrocolloids 27:2 (2012), 411–420.
29. Tanimoto, S.Y., Kinsella, J.E., Enzymic modification of proteins: Effects of transglutaminase cross-linking on some physical properties of beta-lactoglobulin. Journal of Agricultural and Food Chemistry 36:2 (1988), 281–285.
30. Tavares, C., Lopes da Silva, J.A., Rheology of galactomannan–whey protein mixed systems. International Dairy Journal 13:8 (2003), 699–706.
31. Tovar Jiménez, X.A.C., Ainhoa, Téllez Jurado, Alejandro, Abreu Corona, Arturo, Muro Urista, Rosario, C., Traditional methods for whey protein isolation and concentration: Effects on nutritional properties and biological activity. Journal of the Mexican Chemical Society 56:4 (2012), 369–377.
32. 2. The Journal of Physical Chemistry 118 (2014), 6078–6084.
33. Visschers, R.W., de Jongh, H.H.J., Disulphide bond formation in food protein aggregation and gelation. Biotechnology Advances 23:1 (2005), 75–80.
34. Wijayanti, H.B., Oh, H.E., Sharma, R., Deeth, H.C., Reduction of aggregation of beta-lactoglobulin during heating by dihydrolipoic acid. Journal of Dairy Research 80:4 (2013), 383–389.
35. Xiong, Y.L., Influence of pH and ionic environment on thermal aggregation of whey proteins. Journal of Agricultural and Food Chemistry 40:3 (1992), 380–384.
36. Yilmaz-Gemili, A., Electrostatic repulsion enhancement for heat stable, clear whey protein beverages. 2012.
37. Yong, Y.H., Foegeding, E.A., Effects of caseins on thermal stability of bovine β-lactoglobulin. Journal of Agricultural and Food Chemistry 56:21 (2008), 10352–10358.
38. Zayas, J.F., Gelling Properties of Proteins. Functionality of Proteins in Food, 1997, Springer, Berlin, Heidelberg, 339.
39. Zhang, G., Foegeding, E.A., Hardin, C.C., Effect of sulfated polysaccharides on heat-induced structural changes in β-lactoglobulin. Journal of Agricultural and Food Chemistry 52:12 (2004), 3975–3981.
40. Zhang, W., Zhong, Q., Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by sequential enzymatic cross-linking and thermal pretreatments. Journal of Agricultural and Food Chemistry 57:19 (2009), 9181–9189.
41. Zisu, B., Bhaskaracharya, R., Kentish, S., Ashokkumar, M., Ultrasonic processing of dairy systems in large scale reactors. Ultrasound Sonochemistry 17:6 (2010), 1075–1081.