Carp Natural Actomyosin: Thermal Denaturation Mechanism

Sano, Tsuyoshi; Ohno, Tetsuji; Otsuka-Fuchino, Hisako; Matsumoto, Juichiro J.; Tsuchiya, Takahide

doi:10.1111/j.1365-2621.1994.tb08177.x

Cited by 119 publications

(59 citation statements)

References 34 publications

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“…And content of random coil at −12°C and −18°C was slightly higher than 4°C and −1°C. e stabilized α-helix structures were maintained by hydrogen bonds between -CO and NH-of a polypeptide chain [20]. e reduction of α-helix at 4°C and −1°C illustrated that the stability of the secondary structure of myofibrillar protein like hydrogen bonds would be damaged.…”

Section: Secondary Structure Of Myofibrillar Proteins Analysismentioning

confidence: 98%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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e e ects of freezing temperature on the microstructure and moisture migration of beef were investigated, aiming to provide the potential theoretical basis for the beef storage. Drip loss, surface hydrophobicity, and secondary structure of myo brillar proteins, ice crystal, and micro-and ultrastructure of meat were analyzed at 4°C, −1°C, −6°C, −9°C, −12°C, and −18°C, respectively. Results indicated that the drip loss and surface hydrophobicity of samples stored at −12°C were signi cantly lower than that stored at 4°C and −1°C (p < 0.05) and no signi cant di erence with −18°C (p > 0.05). Result from Fourier transform infrared spectroscopy suggested that protein denaturation occurred after storage. ere was an increase in α-helices and decline in random coil at lower temperature (−12°C and −18°C). It was indicated that the samples stored at −12°C and −18°C could e ectively restrain the denaturation of protein and maintain the stability of secondary structure. e analysis of the ice crystal and micro-and ultrastructure of the muscle indicated that the structure of samples stored at −12°C and −18°C had more integrity and was complete than that stored at 4°C and −1°C. e spaces (water "reservoir" and "channel") where was the origination of drip were small. Furthermore, the results of low-eld nuclear magnetic resonance and 1 H magnetic relaxation image showed that the freezing at −12°C could inhibit the migration of immobilized water to free water.

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Section: Secondary Structure Of Myofibrillar Proteins Analysismentioning

confidence: 98%

Effect of Storage Temperatures on the Moisture Migration and Microstructure of Beef

Wang

Mehmood

et al. 2018

Journal of Food Quality

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“…The effect of pH on the secondary structure of scallop actomyosin was also closely related to temperature, with a higher temperature always causing more obvious differences. The a-helical structure is mainly stabilized by hydrogen bonds between the carbonyl oxygen (-CO) and amino hydrogen (NH-) of a polypeptide chain [33,34]. Electrostatic interactions between amino acids also contribute greatly to the stability of secondary structures [35].…”

Section: Effect Of Ph On A-helical Contentmentioning

confidence: 99%

Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

Dong

Zheng

et al. 2014

Fish Sci

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Gelation is an important functional property of protein in meats. In this study, we prepared actomyosin from scallop Patinopecten yessoensis adductor muscles and studied the effects of pH on the physicochemical properties of the actomyosin preparation and on its heat-induced gelforming properties. The results showed that the turbidity and surface hydrophobicity of scallop actomyosin increased with increases in the heating temperature, while the a-helical content concomitantly decreased. Higher turbidity and surface hydrophobicity and lower a-helical content were found to be easily obtained at lower pH values. A high water-holding capacity, strong gel strength, fine gel network and uniform ice crystals were all clearly observed at pH 7.0, indicating that a neutral pH was most beneficial for formation of the heat-induced scallop actomyosin gel. We therefore conclude that both the physicochemical properties of scallop actomyosin and its gelforming ability during the heating process are pH dependent.

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“…[1][2][3][4][5][6][7][8] During the setting, myosin is denatured and aggregated, and simultaneously polymerized by a calcium dependent endogenous TGase* which is responsible for the setting phenomenon and en hance the surimi gelling properties in a great extents.9-13) Thus, the final gel properties seem to be largely determined by a combination of thermal gelling ability of myosin and TGase reaction in the surimi sol.14-16) It is therefore im portant to separate the process of thermally induced gela tion from setting effect induced by TGase to understand the final properties of the two-step heating gel. In this paper we report the effect of the addition of TGase to the heat-denatured surimi, which almost totally lacks gelling ability and setting response, on the recovery of these properties in order to clarify the important roles of TGase and native structure of myosin in the gelling process.…”

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confidence: 99%