Asian-Australasian Journal of Animal Sciences

  • 제16권2호
  • /
  • Pages.269-276
  • /
  • 2003
  • /
  • 1011-2367(pISSN)
  • /
  • 1976-5517(eISSN)
아세아태평양축산학회 (Asian Australasian Association of Animal Production Societies)
권호 표지
DOI QR코드

DOI QR Code

Microbial Transglutaminase Modifies Gel Properties of Porcine Collagen

  • Erwanto, Y. (Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University) ;
  • Kawahara, S. (Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University) ;
  • Katayama, K. (Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University) ;
  • Takenoyama, S. (Kyushu Nutrition Welfare University) ;
  • Fujino, H. (Kyushu Nutrition Welfare University) ;
  • Yamauchi, K. (Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University) ;
  • Morishita, T. (Miyazaki Prefectural Food Research and Development Center) ;
  • Kai, Y. (Minami Nippon Meat Packers, Inc.) ;
  • Watanabe, S. (Minami Nippon Meat Packers, Inc.) ;
  • Muguruma, M. (Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University)
  • 투고 : 2002.07.11
  • 심사 : 2002.10.18
  • 발행 : 2003.02.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

We studied the gel properties of porcine collagen with microbial transglutaminase (MTGase) as a catalyst. A creep meter was used to measure the mechanical properties of gel. The results showed samples with high concentration of MTGase gelled faster than those with a low concentration of MTGase. The gel strength increased with incubation time and the peaks of breaking strength for 0.1, 0.2 and 0.5% MTGase were obtained at 40, 20 and 10 min incubation time, respectively. According to SDS-PAGE, the MTGase was successfully created a collagen polymer with an increase in molecular weight, whereas no change in formation was shown without MTGase. The sample with 0.5% MTGase began to polymerize after 10 or 20 min incubation at $50^{\circ}C$, and complete polymerization occurred after 40-60 min incubation. Scanning electron microscopic analysis revealed that the gel of porcine collagen in the presence of MTGase produced an extremely well cross-linked network. The differential scanning calorimetric analysis showed the peak thermal transition of porcine collagen gel was at $36^{\circ}C$, and that with MTGase no peak was detected during heating from 20 to $120^{\circ}C$. The melting point of porcine collagen gel could be controlled by MTGase concentration, incubation temperature and protein concentration. Knowledge of the structural and physicochemical properties of porcine collagen gel catalyzed with MTGase could facilitate their use in food products.

키워드

참고문헌

  1. Alting A. C., R. J. Hamer, C. G. De Kraif and R. W. Visschers. 2000. Formation of disulfide bonds in acid induced gels of preheated whey protein isolate. J. Agric. Food Chem. 48:5001-5007. https://doi.org/10.1021/jf000474h
  2. Ando, H., M. Adachi, K. Umeda, A. Matsura, M. Nonaka, R. Uchio, H. Tanaka and M. Motoki. 1989. Purification and characteristics of novel food transglutaminase derived from microorganism. Agric. Biol. Chem. 53:2613-2617. https://doi.org/10.1271/bbb1961.53.2613
  3. Ashie, I. N. A. and T. C. Lanier. 1999. High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase. J. Food Sci. 64:704-708. https://doi.org/10.1111/j.1365-2621.1999.tb15115.x
  4. Chronakis, I. S. 2001.Gelation of edible blue-green algae protein isolate (Spirulina platensis strain pacifica): thermal transitions, rheological properties, and molecular forces involved. J. Agric. Food Chem. 49:888-898. https://doi.org/10.1021/jf0005059
  5. Chartoff, R. P. 1997. Thermoplastic polymers. In: Thermal Characterization of Polymeric Materials. 2nd ed., Volume 1, (Ed. E. A. Turi). Academic Press, New York. pp. 483-743.
  6. Erwanto, Y., M. Muguruma, S. Kawahara, T. Tsutsumi , K. Katayama, K.Yamauchi, T. Moroshita, Y. Kai and S. Watanabe. 2002. Effect of heating on polymerization of pig skin collagen using microbial transglutaminase. Asian-Aust. J. Anim. Sci. 15:1204-1209. https://doi.org/10.5713/ajas.2002.1204
  7. Fujisaki, H. and S. Hattori. 1999. Gelatin-binding immunoglobulins in normal bovine serum. Connective Tissue. 31:155-160.
  8. Handa, A., K. Hayashi, H. Shidara and N. Kuroda. 2001. Correlation of the protein structure and gelling properties in dried egg white products. J. Food Sci. 48:3957-3964.
  9. Imm, J. Y., P. Lian and C. M. Lee. 2000. Gelation and water binding properties of transglutaminase-treated skim milk powder. J. Food Sci. 65:200-205. https://doi.org/10.1111/j.1365-2621.2000.tb15979.x
  10. Jiang, S. T., J. F. Hsieh, M. L. Ho and Y. C. Chung. 2000. Microbial transglutaminase affects gel properties of Golden Threadfin-bream and Pollack Surimi. J. Food Sci. 65:694-699. https://doi.org/10.1111/j.1365-2621.2000.tb16074.x
  11. Jiang, S. T., S. Z. Leu and G. J. Tsai. 1998. Cross-linking of Mackerel Surimi actomyosin by microbial transglutaminase and ultraviolet irradiation. J. Agric. Food Chem. 46:5278-5282. https://doi.org/10.1021/jf9806614
  12. Kang, I. J, Y. Matsumura, K. Ikura, M. Motoki, H. Sakamoto and T. Mori. 1994. Gelation and properties of soybean glycinin in a transglutaminase-catalyzed system. J. Agric. Food Chem. 42:159-165. https://doi.org/10.1021/jf00037a028
  13. Kitabatake, N., Y. Tani and E. Doi. 1989. Rheological properties of heat induced ovalbumin gels prepared by two-step and onestep heating methods. J. Food Sci. 54:1632-1638. https://doi.org/10.1111/j.1365-2621.1989.tb05176.x
  14. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. https://doi.org/10.1038/227680a0
  15. Lee, C. and C. Rha. 1979. Rheological properties of proteins in solution. In: Food Texture and Rheology (Ed. Sherman). Academic Press Inc. New York. p. 257.
  16. Lim, L. T., Y. Mine and M. A. Tung. 1999. Barrier and tensile properties of transglutamimnase cross-linked gelatin films as affected by relative humidity, temperature, and glycerol content. J. Food Sci. 64:616-622. https://doi.org/10.1111/j.1365-2621.1999.tb15096.x
  17. Mizuno, A., M. Mitsuiki and M. Motoki. 1999. Glass transition temperature of casein as affected by transglutaminase. J. Food Sci. 64:796-799. https://doi.org/10.1111/j.1365-2621.1999.tb15914.x
  18. Muguruma, M., K. Tsuruoka, H. Fujino, S. Kawahara, K. Yamauchi, S. Matsumura and T. Soeda. 1999. Gel strength enhancement of sausages by treating with microbial transglutaminase. Proceedings of the 45th International Congress of Meat Science and Technology. Yokohama, Japan. 1:138-139.
  19. Muguruma, M., K. Tsuruoka, K. Katayama, Y. Erwanto, S. Kawahara, K. Yamauchi, S. K. Sathe and T. Soeda. 2003. Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Sci. 63:191-197. https://doi.org/10.1016/S0309-1740(02)00070-0
  20. Motoki, M. and K. Seguro. 1998. Transglutaminase and its use for food processing. Trends in Food Sci. Technol. 9:204-210. https://doi.org/10.1016/S0924-2244(98)00038-7
  21. Nomura, Y., S. Toki, Y. Ishii and K. Shirai. 2000. Improvement of material property of shark type I collagen by composing with porcine type I collagen. J. Agric. Food Chem. 48:6332-6336.
  22. Nomura, Y., S. Toki, Y. Ishii and Shirai K. 2001. Physicochemical property of transglutaminase crosslinked pig collagen gel. J. Anim. Sci. 72:322-328.
  23. Nonaka, M., H. Sakamoto, S. Toiguchi, H. Kawajiri, T. Soeda and M. Motoki. 1992. Sodium caseinate and skim milk gels formed by incubation with microbial transglutaminase. J. Food Sci. 57:1214-1218. https://doi.org/10.1111/j.1365-2621.1992.tb11302.x
  24. Sakamoto, H., Y. Kumazawa and M. Motoki. 1994. Strength of protein gels prepared with microbial transglutaminase as related to reaction condition. J. Food Sci. 59:866-871. https://doi.org/10.1111/j.1365-2621.1994.tb08146.x
  25. Sakamoto, H., Y. Kumazawa, S. Toiguchi, K. Seguro, T. Soeda and M. Motoki. 1995. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. J. Food Sci. 60:300-304. https://doi.org/10.1111/j.1365-2621.1995.tb05660.x
  26. Steel, R. G. D. and J. H. Torrie. 1980. Principles and Procedures of Statistics: A Biometrical Approach 2nd ed. McGraw Hill Book Co., Inc., New York.
  27. Takahashi, K. and M. Hattori. 1993. Edible meat casing from reconstruction of collagen-elastin matrix. J. Food Sci. 58:734-738. https://doi.org/10.1111/j.1365-2621.1993.tb09347.x
  28. Takahashi, K., Y. Nakata, K. Someya and M. Hattori. 1999. Improvement of the physical properties of pepsin solubilized elastin-collagen film by cross lingking. Biosci. Biotechnol. and Biochem. 63:2144-2149. https://doi.org/10.1271/bbb.63.2144
  29. Tsai, G. J., S. M. Lin and S. T. Jiang. 1996. Transglutaminase from Streptoverticillium ladakanum and application to minced fish products. J. Food Sci. 61:1234-1238. https://doi.org/10.1111/j.1365-2621.1996.tb10968.x
  30. Tseng, T. F., D. C. Liu and M. T. Chen. 2002. Evaluation of transglutaminase from pig plasma on the quality of milk curd. Asian-Aust. J. Anim. Sci. 15:106-110. https://doi.org/10.5713/ajas.2002.106
  31. Watanabe, K, Y. Tezuka and T. Ishii. 1997. Configuration between re-formed collagen triple helices and artificially introduced cross-links in gelatin gels. Macromolecules. 30:7910-7913. https://doi.org/10.1021/ma9707392
  32. Yoshimura, K., M. Terashima, D. Hozan, T. Ebato, Y. Nomura, Y. Ishii and K. Shirai. 2000. Physical properties of shark gelatin compared with porcine gelatin. J. Agric. Food Chem. 48:2023-2027. https://doi.org/10.1021/jf990887m

피인용 문헌

  1. Effect of Existence of Exogenous Protein on Physicochemical Properties of Heat- and Transglutaminase-induced Bovine Collagen-peptide Gel vol.70, pp.9, 2006, https://doi.org/10.1111/j.1365-2621.2005.tb08310.x
  2. Structure and function of ECM-inspired composite collagen type I scaffolds vol.8, pp.40, 2012, https://doi.org/10.1039/c2sm26134k
  3. Collagen matrix as a tool in studying fibroblastic cell behavior vol.9, pp.4, 2015, https://doi.org/10.1080/19336918.2015.1005469
  4. Application of microbial transglutaminase in meat foods: A review vol.57, pp.10, 2017, https://doi.org/10.1080/10408398.2014.945990
  5. Gelatin-Enabled Microsensor for Pancreatic Trypsin Sensing vol.8, pp.2, 2018, https://doi.org/10.3390/app8020208
  6. Ionically and Enzymatically Dual Cross-Linked Oxidized Alginate Gelatin Hydrogels with Tunable Stiffness and Degradation Behavior for Tissue Engineering vol.6, pp.7, 2003, https://doi.org/10.1021/acsbiomaterials.0c00677