Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate

Food Hydrocolloids

Volumn 30, Issue 1, 2013, Pages 12-18

  Damodaran, Srinivasan ^a   Agyare, Kingsley K ^a,b  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b McCain Foods Limited   (Canada)

Author keywords

Microbial transglutaminase; PH solubility; Thermal stability; Whey protein

Indexed keywords

DISPERSIONS; HYDROPHILICITY; PROTEINS; SOLUBILITY;

DENATURATION TEMPERATURES; HEATSHOCKS; LACTOGLOBULIN; MICROBIAL TRANSGLUTAMINASE; PH ADJUSTMENT; PH-SOLUBILITY; THERMAL DENATURATIONS; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

THERMODYNAMIC STABILITY;

EID: 84861429878     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2012.04.012     Document Type: Article

References (28)

1. Abourmahmoud R., Savello P. Crosslinking of whey protein by transglutaminase. Journal of Dairy Science 1990, 73:256-263.
2. Agyare K.K., Damodaran S. pH-stability and thermal properties of microbial transglutaminase-treated whey protein isolate. Journal of Agricultural and Food Chemistry 2010, 58:1946-1953.
3. Ando H., Adachi M., Umeda K., Matsuura A., Nonaka M., Uchio R., et al. Purification and characteristics of a novel transglutaminase derived from microorganism. Agricultural Biological Chemistry 1989, 53:2613-2617.
4. Childs J.L., Yates M.D., Drake M.A. Sensory properties of meal replacement bars and beverages made from whey and soy proteins. Journal of Food Science 2007, 72:S425-S434.
5. DeWit J.N. Thermal stability and functionality of whey proteins. Journal of Dairy Science 1990, 73:3602-3612.
6. DeWit J.N. Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science 1998, 81:597-608.
7. Dunhill P., Green D.W. Sulphydryl groups and the N↔R conformational change in β-lactoglobulin. Journal of Molecular Biology 1965, 15:147-151.
8. Færgemand M., Murray B.S., Dickinson E. Cross-linking of milk proteins with transglutaminase at the oil-water interface. Journal of Agricultural and Food Chemistry 1997, 45:2514-2519.
9. Fitzsimons S.M., Mulvihill D.M., Morris E.R. Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 2007, 21:638-644.
10. García-Hernández E., Hernández-Arana R.A., Zubillaga R.A., Rojo-Dominguez A. Spectroscopic and thermodynamic evidence for a complex denaturation mechanism of bovine β-lactoglobulin A. Biochemistry and Molecular Biology International 1998, 45:761-768.
11. Han X.Q., Damodaran S. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. Journal of Agricultural and Food Chemistry 1996, 44:1211-1217.
12. Kella N.K.D., Kinsella J.E. Enhanced thermodynamic stability of β-lactoglobulin at low pH. Biochemical Journal 1988, 255:113-118.
13. LaClair C.E., Etzel M.R. Turbidity and protein aggregation in whey protein beverages. Journal of Food Science 2009, 74:C526-C535.
14. LaClair C.E., Etzel M.R. Ingredients and pH are key to clear beverages that contain whey protein. Journal of Food Science 2010, 75:C21-C27.
15. Liu M.X., Damodaran S. Effect of transglutaminase-catalyzed polymerization of β-casein on its emulsifying properties. Journal of Agricultural and Food Chemistry 1999, 47:1514-1519.
16. Lorenzen P.C. Techno-functional properties of transglutaminase-treated milk proteins. Milchwissenschaft 2000, 55:667-670.
17. Prabakaran S., Damodaran S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. Journal of Agricultural and Food Chemistry 1997, 45:4303-4308.
18. Privalov P.L., Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure. A calorimetric study. Journal of Molecular Biology 1974, 86:665-684.
19. Soeda T., Hokazono P., Kasagi T., Sakamoto M. Improvement of functional properties of WPC by microbial transglutaminase. Journal of the Japan Society of Food Science 2006, 53:74-79.
20. Song K.B., Damodaran S. Influence of electrostatic forces on the adsorption of succinylated β-lactoglobulin at the air-water interface. Langmuir 1991, 7:2737-2742.
21. Tang C.H., Ma C.-Y. Modulation of the thermal stability of β-lactoglobulin by transglutaminase treatment. European Food Research and Technology 2007, 225:649-652.
22. Tang C.H., Yang X.Q., Chen Z., Wu H., Peng Z.Y. Physicochemical and structural properties of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 2005, 29:402-421.
23. Tanimoto S.-Y., Kinsella J.E. Enzymatic modification of proteins: effects of transglutaminase cross-linking on some physical properties of β-lactoglobulin. Journal of Agricultural and Food Chemistry 1988, 36:281-285.
24. Tolkach A., Kulozik U. Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Lait 2007, 87:301-315.
25. Wada R., Fujita Y., Kitabatake N. Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochimica Biophysica Acta 2006, 1760:841-847.
26. Wang C.H., Damodaran S. Thermal gelation of globular proteins: weight-average molecular weight dependence of gel strength. Journal of Agricultural and Food Chemistry 1990, 38:1157-1164.
27. Yokoyama K., Nio N., Kikuchi Y. Properties and applications of microbial transglutaminase. Applied Microbiology and Biotechnology 2004, 64:447-454.
28. Zhu H., Damodaran S. Heat-induced conformational changes in whey protein isolate and its relationship to foaming properties. Journal of Agricultural and Food Chemistry 1994, 42:846-855.