Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef

Meat Science

Volumn 82, Issue 2, 2009, Pages 170-178

  Ahhmed, Abdulatef Mrghni ^a,b   Nasu, Tetsuo ^a   Huy, Dang Quang ^a   Tomisaka, Yoshito ^a   Kawahara, Satoshi ^a   Muguruma, Michio ^a,b  

^a UNIVERSITY OF MIYAZAKI   (Japan)

^b KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

( Glultamyl)lysine content; Chicken and beef; Natural actomyosin; Rheological and physiochemical properties; Transglutaminase

Indexed keywords

EID: 62349141549     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.01.007     Document Type: Article

References (28)

1. Ahhmed M.A., Kuroda R., Kawahara S., Ohta K., Nakade K., Aoki T., et al. Dependence of microbial transglutaminase on meat type in myofibrillar proteins cross-linking. Food Chemistry 112 (2009) 354-361
2. Ahhmed, M. A., Kawahara, S., & Muguruma, M. (2008) Evaluation of the discrepancy of physiochemical and rheological properties of cross-linked myosin B proteins and biopolymers catalyzed by transglutaminase in meats. In Proceeding of the 54th International Congress of Meat Science and Technology, (p. 117), 10-15 August 2008, Cape Town, South Africa.
3. Ahhmed M.A., Kawahara S., Ohta K., Nakade K., Soeda T., and Muguruma M. Differentiation in improvements of gel strength in chicken and beef sausages induced by transglutaminase. Meat Science 76 (2007) 455-462
4. Ando H., Adachi M., Umeda K., Matsuura A., Nonaka M., Uchio K., Tanaka H., and Motoki M. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agricultural Biological Chemistry 53 (1989) 2613-2617
5. Asghar A., Morita J., Samejima K., and Yasui T. Biochemical and functional characteristics of myosin from Red and White muscles of chicken as influenced by nutritional stress. Agricultural Biological Chemistry 48 (1984) 2217-2224
6. Benjakul S., Vissanguan W., and Pecharat S. Suwari gel properties as affected by transglutaminase activators and inhibitors. Food Chemistry 85 (2004) 91-99
7. Choe I., Morita J., Yamamoto K., Samejima K., and Yasui T. Heat-induced gelation of myosins/subfragments from chicken leg and breast muscles at high ionic strength and low pH. Journal Food Science 56 (1991) 884-891
8. Dondero M., Figueroa V., Morales X., and Curotto E. Transglutaminase effects on gelation capacity of thermally induced beef protein gels. Food Chemistry 99 (2006) 546-554
9. Erwanto Y., Kawahara S., Katayama K., Ahhmed M.A., Yamauchi K., Chin K.B., and Muguruma M. Effect of existence of exogenous protein on physicochemical properties of heat- and transglutaminase-induced bovine collagen-peptide gel. Journal of Food Science 70 (2005) E505-E509
10. Folk E.J., and Finlayson S.J. The epsilon-(gamma-glutamyl)lysine crossly and the catalytic role of transglutaminases. Advanced Protein Chemistry 31 (1977) 1-133
11. Griffin M.R., Casadio C., and Bergamini M. Transglutaminases: Nature's biological glues. Biochemistry Journal 368 (2002) 377-396
12. Hayakawa I., Kajihara J., Morikawa K., Oda M., and Fujio Y. Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals. Journal of Food Science 50 (1985) 486-491
13. Kanaji T., Ozaki H., Takao T., Kawajiri H., Ide H., Makoto M., and Shimonishi Y. Primary structure of microbial transglutaminase from Sterptoverticillium sp. Strain s-8112. Journal of Biological Chemistry 268 (1993) 11565-11572
14. Kawahara S., Ahhmed M.A., Ohta K., Nakade K., and Muguruma M. Inconsistency in the improvements of gel strength in chicken and pork sausages include by microbial transglutaminase. Asian-Australasian Journal of Animal Science 20 (2007) 1285-1291
15. Keeton J.T., and Eddy S. Chemical and physical characteristics of meat. In: Jensen W.K., Devine C., and Dikeman M. (Eds). Encyclopedia of meat sciences Vol. 1 (2004), Elsevier academic press, Oxford, England 210-238
16. Kikuchi Y., Date M., Yokoyama K., Umezawa Y., and Matsui H. Secretion of active-form Streptoverticillium mobaraense transglutaminase by corynebacterium glutamicum: Processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Applied Environmental Microbiology 69 (2003) 358-366
17. Kumazawa Y., Seguro K., Takamura M., and Motoki M. Formation of ε-(γ-glutamyl) lysine cross-link in cured horse mackerel meat induced by drying. Journal of Food Science 58 (1993) 1062-1064
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
19. Lan Y.H., Novakofski E.J., McCusker H.R., Brewer S.M., Carr R.T., and McKeith K.F. Thermal gelation of myofibrils from pork, bee, fish, chicken and turkey. Journal of Food Science 60 (1995) 941-945
20. Lin C.L., and Ito T. Flow behavior and scanning electron microscopy of myosin B, soya protein components and mixtures at varying temperatures. Journal of Food Technology 21 (1986) 133-149
21. Müller W.D. The technology of cooked cured products. Fleischwirtschaft 69 (1989) 1425-1428
22. Nishimura T., Okitani A., Rhyu M.R., and Kato H. Survey of neutral amino peptidases in bovine, porcine and chicken skeletal muscles. Agricultural Biological Chemistry 54 (1990) 2769-2775
23. Ooizumi T., and Xing L.Y. Biochemical susceptibility of myosin in chicken myofibrils subjected to hydroxyl radical oxidizing systems. Journal of Agricultural Food Chemistry 52 (2004) 4303-4307
24. Pollard T.D. A falling ball apparatus to measure filament cross-linking. Methods in cell biology Vol. 24 (1982), Academic Press Inc., London, England 301-308
25. Resurreccion A.V.A. Cookery of muscle food. In: Kinsman D.M., Kotula A.W., and Breidenstein B.C. (Eds). Muscle foods (1994), Chapman and Hall Inc, New York, USA 406-429
26. Sakamoto H., Kumazawa Y., Toiguchi 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 (1995) 300-304
27. Tomita S. Studies on the fluorometric analysis of polyelectrolytes (I) Protein. Japan National Chemistry Laboratory of Industry 58 (1963) 99-107
28. Umezawa Y., Yokoyama K., Kikuchi Y., Date M., Ito K., Yoshimoto T., and Matsui H. Novel prolyl tri/tetra-peptidyl aminopeptidase from Streptomyces mobaraensis: Substrate specificity and enzyme gene cloning. Journal of Biochemistry 136 (2004) 293-300