- Volume 16 Issue 2
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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
Supported by : Miyazaki Prefectural Industrial Support Foundation
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