Transglutaminase effects on gelation capacity of thermally induced beef protein gels

Food Chemistry

Volumn 99, Issue 3, 2006, Pages 546-554

  Dondero, Marta ^a   Figueroa, Valeria ^a   Morales, Ximena ^a   Curotto, Emilia ^a  

^a PONTIFICIA UNIVERSIDAD CATÓLICA DE VALPARAÍSO   (Chile)

Author keywords

Beef; Gelation capacity; Surimi; Texture; Transglutaminase

Indexed keywords

LYSINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

ARTICLE; CHEMICAL BOND; CHILEAN JACK MACKEREL; COOKING; ELECTROPHORESIS; ENZYME ACTIVITY; FISH; FOOD; FOOD ANALYSIS; FOOD QUALITY; FOOD TEXTURE; GELATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INCUBATION TEMPERATURE; INCUBATION TIME; MEAT; POLYACRYLAMIDE GEL ELECTROPHORESIS; SURIMI;

TRACHURUS MURPHYI;

EID: 33646522217     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2005.08.022     Document Type: Article

References (36)

1. Asagami T., Ogiwara M., Wakameda A., and Noguchi S. Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of fish species. Fisheries Science 61 2 (1995) 267-272
2. Curotto E., Canales L., Alviña P., and Dondero M. Partial purification and characterization of alkaline thermoestable proteases of jack mackerel (Trachurus murphyi). Journal of Aquatic Food Product Technology 8 2 (1999) 25-37
3. De Backer-Royer C., Traorë F., and Meunier J. Polymerization of meat and soybean proteins by human placental calcium-activated factor XIII. Journal of Agricultural Food Chemistry 40 11 (1992) 2052-2056
4. De Jong G., and Koppelman S. Transglutaminase catalyzed reactions: impact on food applications. Journal of Food Science 67 8 (2002) 2798-2806
5. Dondero M., Concha P., and Curotto E. Inhibición de proteasas en geles de surimi de jurel. Food Science and Technology International 5 3 (1999) 203-214
6. Dondero M., Curotto E., and Figueroa V. Transglutaminase effects on gelation of jack mackerel surimi. Food Science and Technology International 8 1 (2002) 49-54
7. Figueroa, V. (1997). Comportamiento functional en mezclas de proteinas de jurel y vacuno. Tesis de Ingeniero de Alimentos. Escuela de Alimentos. Pontificia Universidad Católica de Valparaíso. Chile.
8. Griffin M., Wilson J., and Lorand A. High-pressure liquid chromatographic procedure for the determination of ε(γ-glutamyl)lysine in protein. Analytical Biochemistry 58 (1982) 37-49
9. Han X., and Damodaran S. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. Journal of Agricultural Food Chemistry 44 (1996) 1211-1217
10. Kim S., Carpenter J., Lanier T., and Wickler L. Polymerization of beef actomyosin induced by transglutaminase. Journal of Food Science 58 3 (1993) 473-474
11. Kim S., Carpenter J., Lanier T., and Wickler L. Setting response of Alaska pollock surimi compared with beef myofibrils. Journal of Food Science 58 3 (1993) 531-534
12. Kuraishi C.H., Sakamoto J., Yamazaki K., Sussan Y., Kuhara C.H., and Soeda T. Production of restructured meat using microbial transglutaminase without salt or cooking. Journal of Food Science 62 3 (1998) 488-490
13. Kuraishi C., Yamasaki K., and Susa Y. Transglutaminase: its utilization in the food industry. Food Reviews International 17 2 (2001) 221-246
14. Kumazawa Y., Numasawa T., Seguro K., and Motoki M. Suppression of surimi gel setting by transglutaminase inhibitors. Journal of Food Science 60 4 (1995) 715-717
15. Kumasawa Y., Seguro M., Tamakura M., and Motoki M. Formation of ε-(γ-glutamyl)lysine crosslink in cured horse mackerel meat induced by drying. Journal of Food Science 58 5 (1997) 1062-1064
16. Kurth L., and Rogers P. Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. Journal of Food Science 49 4 (1984) 573-589
17. Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
18. Motoki M., and Seguro K. Transglutaminase and its use for food processing. Trends in Food Science and Technology 9 (1998) 204-210
19. Muñoz, C. (1999). Extracción, evaluación y caracterización parcial de la enzima TGasa en músculo blanco de jurel, proteínas miofibrilares de carne y surimi de jurel. Tesis Bioquímica. Instituto de Química. Pontificia Universidad Católica de Valparaíso. Chile.
20. Nishimoto S., Hashimoto A., Seki N., and Arai K. Setting of mixed salted paste of two fish species in relation to cross-linking of myosin heavy chain. Nippon Suissan Gakkaishi 54 (1987) 1227-1235
21. Nishimoto S., Hashimoto A., Seki N., and Arai K. Setting of mixed salt paste of two fish species in relation to cross-linking reaction of myosin heavy chain. Nippon Suissan Gakkaishi 54 (1988) 1789-1793
22. Niwa E., Suzumura T., Nowsad A., and Katoh S. Setting of actomyosin paste containing few amount of transglutaminase. Nippon Suisan Gakkaishi 59 12 (1993) 2043-2046
23. Numata M., Yamada H., Nakamura T., and Muguruma M. Studies on application of transglutaminase to meta and meta products. I. The effect of Transglutaminase on heat induced gelation and water holding capacity of myosin B. Journal of Japanese Society of Food Science and Technology 36 (1989) 832-838
24. Pietrasik Z., and Li-Chan E. Response surface methodology on the effects of sal, microbial transglutaminase and heating temperature on pork batter gel properties. Food Research International 35 (2002) 387-396
25. Ramírez-Suarez J., and Xiong Y. Effect of transglutaminase-induced cross-linking on gelation of myofibrilar/soy protein mixtures. Meat Science 65 (2003) 899-907
26. Rodgers M., Karr T., Biedermann K., Ueno U., and Harrigton W. Thermal stability of myosin rod from various species. Biochemistry 26 (1987) 8703
27. Sakamoto H., Kumasawa Y., and Motoki M. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. Journal of Food Science 59 4 (1994) 866-871
28. Sakamoto H., Kumazawa Y., Toguchi S., Seguro K., Soeda T., and Motoki M. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. Journal of Food Science 60 2 (1995) 300-304
29. Samejima K., Egelandsdal B., and Fretheim K. Heat gelation properties and protein extractability of beef myofibrils. Journal of Food Science 50 5 (1985) 1540-1544
30. Seguro K., Kumasawa Y., Ohtsuka T., Seiichiro T., and Motoki M. Microbial Transglutaminase and epsylon-(gamma-glutamyl) lysine crosslink effects on elastic properties of kamaboko gels. Journal of Food Science 60 2 (1995) 305-311
31. Torley P., and Lanier T. Seafood Science and Technology. In: Graham Bligh E. (Ed). Setting ability of salted beef/pollock surimi mixtures (1991), Fishing News Books Ltd., Oxford, UK 305-316
32. Trout G., and Schmidt G. Effects of phosphates on the functional properties of restructured beef rolls: The role of pH, ionic strength and phosphate type. Journal of Food Science 51 6 (1986) 1416-1423
33. Tsai G., Lin S., and Jiang S. Transglutaminase from Stretoverticillium ladakanum and application to minced fish product. Journal of Food Science 61 6 (1996) 1234-1238
34. Tseng T., Liu D., and Chen M. Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Science 55 (2000) 427-431
35. Yanusaga K., Abe Y., Yamasawa M., and Arai K. Heat-induced change in myosin heavy chains in SALT ground meat with a food additive containing transglutaminase. Nippon Suisan Gakkaishi 64 4 (1996) 659-668
36. Zhu Y., Rinzema A., Tramper J., and Bold J. Microbial transglutaminase. A review of its production and application in food processing. Applied Microbiology and Biotechnology 44 (1995) 277-282