Crosslinking of milk whey proteins by transglutaminase

Process Biochemistry

Volumn 43, Issue 7, 2008, Pages 788-794

  Gauche, Cony ^a   Vieira, Joana T C ^a   Ogliari, Paulo J ^a   Bordignon Luiz, Marilde T ^a  

^a CAL   (Brazil)

Author keywords

Lactalbumin; Lactoglobulin; Crosslinking; Electrophoresis; Rheology; Transglutaminase

Indexed keywords

CROSSLINKING; ELECTROPHORESIS; ENZYME ACTIVITY; POLYMERIZATION; RHEOLOGY; VISCOSITY;

LACTALBUMIN; LACTOGLOBULIN; TRANSGLUTAMINASE;

PROTEINS;

EID: 44249101350     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.04.004     Document Type: Article

References (40)

1. Motoki M., and Seguro K. Transglutaminase and its use for food processing. Trends Food Sci Technol 9 (1998) 204-210
2. Kuraishi C., Yamazaki K., and Susa Y. Transglutaminase: its utilization in the food industry. Food Rev Int 17 (2001) 221-246
3. Nielsen G.S., Petersen B.R., and Moller A.J. Impact of salt, phosphate and temperature on the effect of a transglutaminase (F XIIIA) on the texture of restructured meat. Meat Sci 41 (1995) 293-299
4. Ando H., Adachi M., Umeda K., Matsura A., Nonaka M., Uchio R., et al. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric Biol Chem 53 (1989) 2613-2617
5. Mugurama M., Tsuruoka K., Katamayma K., Erwanto Y., Kawahara S., Yamauchi K., et al. Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Sci 63 (2003) 191-197
6. Kruif C.G., Tuinier R., Holt C., Timmins P.A., and Rollema H.S. Physicochemical study of κ- and β-casein dispersions and the effect of cross-linking by transglutaminase. Langmuir 18 (2002) 4885-4891
7. Faergemand M., Murray B.S., Dickinson E., and Qvist K.B. Cross-linking of adsorbed casein films with transglutaminase. Int Dairy J 9 (1999) 343-346
8. Collar C., Bollaín C., and Angioloni A. Significance of microbial transglutaminase on the sensory, mechanical and crumb grain pattern of enzyme supplemented fresh pan breads. J Food Eng 70 (2005) 479-488
9. Bauer N., Koehler P., Wieser H., and Schieberle P. Studies on effects of microbial transglutaminase on gluten proteins of wheat. II. Rheological properties. Cereal Chem 80 (2003) 787-790
10. Larré C., Denery-Papini D., Popineau Y., Deshayes G., Desserme G., and Lefebvre J. Biochemical analysis and rheological properties of gluten modified by transglutaminase. Cereal Chem 77 (2000) 121-127
11. Siu N., Ma C., and Mine Y. Physicochemical and structural properties of oat globulin polymers formed by a microbial transglutaminase. J Agric Food Chem 50 (2002) 2660-2665
12. Siu N., Ma C., Mock W., and Mine Y. Functional properties of oat globulin modified by a calcium-independent microbial transglutaminase. J Agric Food Chem 50 (2002) 2666-2670
13. Lantto R., Puolanne E., Kalkkinen N., Buchert J., and Autio K. Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability. J Agric Food Chem 53 (2005) 9231-9237
14. Tseng T., Chen M., and Liu D. Purification of transglutaminase and its effects on myosin heavy chain and actin of spent hens. Meat Sci 60 (2002) 267-270
15. Jiang S., Leu S., and Tsai G. Cross-linking of mackerel surimi actomyosin by microbial transglutaminase and ultraviolet irradiation. J Agric Food Chem 46 (1998) 5278-5282
16. Gerrard J.A., Newberry M.P., Ross M., Wilson A.J., Fayle S.E., and Kavale S. Pastry lift and croissant volume as affected by microbial transglutaminase. J Food Sci 65 (2000) 312-314
17. Gerrard J.A., Fayle S.E., Brown P.K., Sutton K.H., Simmons L., and Rasiah I. Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough. J Food Sci 66 (2001) 782-786
18. Yasir S.B.M., Sutton K.H., Newberry M.P., Andrews N.R., and Gerrard J.A. The impact of transglutaminase on soy proteins and tofu texture. Food Chem 104 (2007) 1491-1501
19. Rodriguez-Nogales J.M. Effect of preheat treatment on the transglutaminase-catalyzed cross-linking of goat milk proteins. Process Biochem 41 (2006) 430-437
20. O'Sullivan M.M., Kelly A.L., and Fox P.F. Effect of transglutaminase on the heat stability of milk: a possible mechanism. J Dairy Sci 85 (2002) 1-7
21. Sharma R., Lorenzen P.C., and Qvist K.B. Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. Int Dairy J 1 (2001) 785-793
22. Dickinson E., and Yamamoto Y. Rheology of milk protein gels and protein-stabilized emulsion gels cross-linked with transglutaminase. J Agric Food Chem 44 (1996) 1371-1377
23. Rodriguez-Nogales J.M. Enzymatic cross-linking of ewe's milk proteins by transglutaminase. Eur Food Res Technol (2005) 1-8
24. Sharma R., Zakora M., and Qvist K.B. Susceptibility of an industrial α-lactalbumin concentrate to cross-linking by microbial transglutaminase. Int Dairy J 12 (2002) 1005-1012
25. Han X.-D., and Damodaran S. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. J Agric Food Chem 44 (1996) 1211-1217
26. Montgomery D. Design and analysis of experiments (1991), John Wiley & Sons, New York
27. AOAC. Official Methods of Analysis of AOAC International. 18th ed. (2005), AOAC, Maryland
28. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
29. Wilcox C.P., and Swaisgood H.E. Modification of the rheological properties of whey protein isolate through the use of an immobilized transglutaminase. J Agric Food Chem 50 (2002) 5546-5551
30. Teófilo R.F., and Ferreira M.M.C. Quimiometria II: Planilhas eletrônicas para cálculos de planejamentos experimentais, um tutorial. Quím Nova 29 (2006) 338-350
31. Morr C., and Há E.W. Whey protein concentrates and isolates processing and functional properties critical reviews. Food Sci Nutr 33 (1993) 431-476
32. Dickinson E. Enzymatic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends Food Sci Technol 8 (1997) 334-339
33. Nieuwenhuizen W.F., Dekker H.L., Koning L.J., Gröneveld T., Koster C.G., and Jong G.A.H. Modification of glutamine and lysine residues in holo and apo-α-lactalbumin with microbial transglutaminase. J Agric Food Chem 51 (2003) 7132-7139
34. Eissa A.S., Bisram S., and Khan S.A. Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme. J Agric Food Chem 52 (2004) 4456-4464
35. 2+-independent microbial transglutaminase from Streptomyces lydicus. Food Hydrocolloids 11 (1997) 19-25
36. Lizarraga M.S., De Piante Vicin D., González R., Rubiolo A., and Santiago L.G. Rheological behaviour of whey protein concentrate and λ-carrageenan aqueous mixtures. Food Hydrocolloids 20 (2006) 740-748
37. Patocka G., Cervenkova R., Narine S., and Jelen P. Rheological behaviour of dairy products as affected by soluble whey protein isolate. Int Dairy J 16 (2006) 399-405
38. Rao M.A. Rheology of fluid and semisolid foods: principles and applications (1999), An Aspen Publication, New York
39. Piau J.M., and Debiane K. Consistometers rheometry of power-law viscous fluids. J Non-Newtonian Fluid Mech 127 (2005) 213-224
40. Babiker E.E. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chem 70 (2000) 139-145