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Effect of Heating on Polymerization of Pig Skin Collagen Using Microbial Transglutaminase
Erwanto, Yuny,Muguruma, Michio,Kawahara, Satoshi,Tsutsumi, Takahiko,Katayama, Kazunori,Yamauchi, Kiyoshi,Morishita, Toshiro,Morishita, Toshiro,Watanabe, Shohei Asian Australasian Association of Animal Productio 2002 Animal Bioscience Vol.15 No.8
Polymerization of heated or unheated pig skin collagen using microbial transglutaminase (MTGase) was investigated. Pig skin collagen samples were heated or left unheated, then enzymatically polymerized with MTGase. SDS-PAGE was conducted to confirm the intermolecular polymer and the results showed similar bands between samples without MTGase and unheated samples with MTGase. The polymerized product of pig skin collagen was not formed in unheated samples, even when MTGase was added during incubation. Different results were obtained from samples heated at $80^{\circ}C$ and $100^{\circ}C$ for 2 min, whereas the SDS-PAGE pattern indicated that a polymer band was generated in both cases. The heat treatment successfully modified the native structure of collagen and also made collagen more reactable in the MTGase polymerization system. Scanning Electron Microscope (SEM) investigation of pig skin collagen showed a biopolymer structure through intermolecular collagen crosslinking, while there were no intermolecular crosslinks in samples not treated with MTGase. There were no significant differences in fibril diameter between treated samples and controls. These results suggest that heat treatment of native pig skin collagen enhanced the polymerization capability of MTGase.
Katayama, Kazunori,Fuchu, Hidetaka,Sugiyama, Masaaki,Kawahara, Satoshi,Yamauchi, Kiyoshi,Kawamura, Yukio,Muguruma, Michio Asian Australasian Association of Animal Productio 2003 Animal Bioscience Vol.16 No.9
In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.