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Effects of high intensity unltrasound on structural and physicochemical properties of myosin from silver carp
Affiliation:1. College of Food Science and Technology, Huazhong Agricultural University/National R & D Branch Center for Conventional Freshwater Fish Processing (Wuhan), Wuhan, Hubei Province 430070, PR China;2. Collaborative Innovation Center for Efficient and Health Production of Fisheries in Hunan Province, Changde 415000, PR China;1. Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan;2. AminoScience Laboratories, Ajinomoto Inc., 1-1 Kawasaki, Japan;3. Alliance Protein Laboratories, San Diego, CA 92121, USA;1. State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, China;2. School of Applied Chemistry and Biological Technology, Shenzhen Polytechnic, Shenzhen, 518055, China;3. Fujian Anjoyfood Share Co. Ltd., Xiamen, 361022, China;4. Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, 214122, China;1. College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China;2. State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, PR China;3. Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, PR China;1. College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei, 430070, China;2. Engineering Research Center of Green Development for Conventional Aquatic Biological Industry in the Yangtze River Economic Belt, Ministry of Education, Wuhan, 430070, China;3. National R & D Branch Center for Conventional Freshwater Fish Processing, Wuhan, Hubei, 430070, China
Abstract:Myosin from silver carp was sonicated with varying power output (100, 150, 200 and 250 W) for 3, 6, 9, and 12 min. The changes in the structure and physicochemical properties of myosin were evaluated by dynamic light scattering, SDS-PAGE and some physicochemical indexes. The ultrasound treatments induced a significant conversion of myosin aggregates to smaller ones with a more uniform distribution, and obvious enhancement in solubility. The structure of myosin was also notably changed by sonication, with a decrease in Ca2+-ATPase activity and SH content, and an increase in surface hydrophobicity. Furthermore, SH groups were oxidized, leading to a decrease in reactive SH and total SH contents. SDS-PAGE analysis revealed that ultrasound could induce the degradation of myosin heavy chain and change the protein fraction of myosin. Collectively, the ultrasonic treatment of 100 W for 3 min showed slight influence on the SH content, S0-ANS, and electrophoretic patterns, and the extent of changes in myosin structure and physicochemical properties tended to increase with ultrasonic power and time. The integrated data indicate that ultrasonic treatment can facilitate the improvement of the solubility and dispersion of myosin, but the choice of a suitable ultrasonic condition to avoid oxidation and degradation of myosin is very important.
Keywords:High intensity ultrasound  Myosin  Structure  Interaction  Physicochemical property
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