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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.
Numerical Study on Loss Mechanism in Rear Rotor of Contra-Rotating Axial Flow Pump
De Zhang,Yusuke Katayama,Satoshi Watanabe,Shin-Ichi Tsuda,Akinori Furukawa 한국유체기계학회 2020 International journal of fluid machinery and syste Vol.13 No.1
It is known that higher efficiency can be achieved with reduced specific speed design of rear rotor in contra-rotating axial flow pump. To investigate the mechanism of increased efficiency with the reduced specific speed of rear rotor, three models with different specific-speed rear rotors are designed with the conventional method, and the flow fields are simulated by unsteady RANS simulation. To analyze the loss generation mechanism, two loss evaluation methods based on the entropy production rate and the material-derivative of rothalpy are employed. It is found that, although the both methods qualitatively estimate the total loss through the rear rotor, the derivative of rothalpy can give much better quantitative prediction of the losses. Two distinct flow features are observed in the rear rotor, the corner separation at the hub corner of blades and the tip leakage vortex, both of which are responsible for the loss generation. With the evaluation of local loss generation based on the material derivative of rothalpy, the loss contribution of corner separation is found to be very small compared with that due to the tip leakage vortex. The tip leakage vortex structure in high specific speed rear rotor shows the strong interaction with the leading edge of adjacent blade, which seems to strengthen the blockage effect in the tip region. This is relieved in the lower specific speed rear rotor, resulting in the achievement of higher efficiency with it.
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.