- Volume 16 Issue 2
Microbial Transglutaminase Modifies Gel Properties of Porcine Collagen
DOI QR Code
Erwanto, Y.;Kawahara, S.;Katayama, K.;Takenoyama, S.;Fujino, H.;Yamauchi, K.;Morishita, T.;Kai, Y.;Watanabe, S.;Muguruma, M.
- 투고 : 2002.07.11
- 심사 : 2002.10.18
- 발행 : 2003.02.01
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
Porcine Collagen Gel;Microbial Transglutaminase;Structural and Physicochemical Properties;Melting P
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- Fujisaki, H. and S. Hattori. 1999. Gelatin-binding immunoglobulins in normal bovine serum. Connective Tissue. 31:155-160.
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
- 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
- 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.
- Nomura, Y., S. Toki, Y. Ishii and Shirai K. 2001. Physicochemical property of transglutaminase crosslinked pig collagen gel. J. Anim. Sci. 72:322-328.
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