Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure.

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.