Abstract
The effects of high pressure (100–500MPa) 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 760cm−1 band showed a maximum value at 200MPa, indicating that 200MPa was the optimum pressure for hydrophobic interactions. Hydrogen bonding of MP gel was strengthened at pressures of 300MPa 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 200MPa was the optimum pressure for the water holding capacity of MP gel.
Published Version
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