title: Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure.
abstract: The effects of high pressure (100-500 MPa) on chemical forces and water holding capacity of heat-induced myofibrillar protein (MP) gel were investigated. As pressure increased, total sulfhydryl (SH) group content decreased and absolute value of zeta potential increased, which suggested the formation of disulfide bonds and increased the strength of electrostatic repulsion. Surface hydrophobicity and normalized intensity of the 760 cm(-1) band showed a maximum value at 200 MPa, indicating that 200 MPa was the optimum pressure for hydrophobic interactions. Hydrogen bonding of MP gel was strengthened at pressures of 300 MPa and above. Bound water (T2b) had lower water mobility and was more closely associated with proteins. Free water (T22) had higher water mobility. More free water was attracted by proteins or trapped in gel structure, and transferred to bound or immobilized water as pressure increased. A value of 200 MPa was the optimum pressure for the water holding capacity of MP gel.
authors.affiliation: 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, China.
authors.forename: Ziye
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: 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, China. Electronic address: yulingy@sina.com.
authors.forename: Yuling
authors.initials: Y
authors.lastname: Yang
authors.affiliation: 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, China.
authors.forename: Xiaozhi
authors.initials: X
authors.lastname: Tang
authors.affiliation: 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, China.
authors.forename: Yinji
authors.initials: Y
authors.lastname: Chen
authors.affiliation: 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, China.
authors.forename: Yuan
authors.initials: Y
authors.lastname: You
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D006358:Hot Temperature; D006860:Hydrogen Bonding; D011312:Pressure; D055672:Static Electricity; D014867:Water / Q000737:chemistry*; D000099163:Myosin Binding Protein C
chemical_list: D002352:Carrier Proteins; D014867:Water; D000099163:Myosin Binding Protein C
keywords: Electrostatic interactions; High pressure; Hydrogen bond; Low field NMR; Myofibrillar protein; Water holding capacity