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)
  • Received : 2002.07.11
  • Accepted : 2002.10.18
  • Published : 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 $50^{\circ}C$, 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.


Supported by : Miyazaki Prefectural Industrial Support Foundation


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