title: Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel.
abstract: The effects of high intensity ultrasound (HIU) modification (power: 200, 400, 600, 800 and 1000W, corresponding to intensities of: 88, 117, 150, 173 and 193Wcm-2) on the physicochemical properties of myofibrillar protein (MP) and water in MP gel were studied. As the HIU power increased, the solubility, surface hydrophobicity and absolute value of the zeta potential increased, while turbidity and total sulfhydryl (SH) group content decreased. The G' and G″ of MP during thermal gelation decreased as ultrasound intensity increased due to greater protein denaturation. Low field NMR data showed that bound water (T2b) had lower water mobility and was more closely associated with proteins in HIU treated MP gel, while the proportions of immobilized water (PT21) and free water (PT22) had their maximum and minimum value, respectively, at 600W. Moderate HIU (≦600W) treatments had denser and uniform gel microstructure, which improved water holding capacity (WHC) of the gels, while stronger HIU (>600W) treatments had larger and irregular gel microstructures, accompanied by decreased WHC.
authors: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, China.
authors: Ziye
authors: Z
authors: Zhang
authors: Department of Food Science, Cornell University, Ithaca, NY 14853-7201, USA.
authors: Joe M
authors: JM
authors: Regenstein
authors: State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, China. Electronic address: zhoupeng@jiangnan.edu.cn.
authors: Peng
authors: P
authors: Zhou
authors: College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, China. Electronic address: yulingy@163.com.
authors: Yuling
authors: Y
authors: Yang
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D005782:Gels; D057927:Hydrophobic and Hydrophilic Interactions; D009124:Muscle Proteins / Q000737:chemistry*; D010316:Particle Size; D012995:Solubility; D013438:Sulfhydryl Compounds / Q000737:chemistry; D000069453:Ultrasonic Waves; D014867:Water / Q000737:chemistry*
chemical_list: D005782:Gels; D009124:Muscle Proteins; D013438:Sulfhydryl Compounds; D014867:Water
keywords: Bound water; High intensity ultrasound; Low field NMR; Myofibrillar gels; Myofibrillar protein; Water holding capacity