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T.Yamauchi,H.Hirano 한국펄프·종이공학회 1999 한국펄프종이학회 기타 간행물 Vol.- No.-
J-integral at the onset of stable crack growth (Jc) was examined on the double edge notched specimens of machine-glazed paper. comparing with J-integral at the onset of unstable crack growth i. e. at the maximum load point (Jmax). Jmax depends on the specimen width and is considerably larger thin Jc. On the other hand. Jc is nearly constant independent of the width and thus is regarded as a material property for evaluating fracture toughness of paper as long as a stable crack grows before the maximum load point. The specimen geometry employed in this study fulfills the condition required for the single specimen method of J-integral determination.
Microbial Transglutaminase Modifies Gel Properties of Porcine Collagen
Erwanto, Y.,Kawahara, S.,Katayama, K.,Takenoyama, S.,Fujino, H.,Yamauchi, K.,Morishita, T.,Kai, Y.,Watanabe, S.,Muguruma, M. Asian Australasian Association of Animal Productio 2003 Animal Bioscience Vol.16 No.2
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.