<scp>l</scp>-histidine improves water retention of heat-induced gel of chicken breast myofibrillar proteins in low ionic strength solution

Summary The effects of 5 mm l-histidine (l-His) on water-binding capacity, gel strength, thermal gelling properties of chicken breast myofibrillar proteins (MPs) in 1 mm NaCl or 0.6 m NaCl solutions (pH 7.0) were investigated. l-His could significantly increase the solubility and thermal gelling ability of MPs in 1 mm NaCl. l-His at 1 mm NaCl shortened the water relaxation time and decreased the water mobility of MPs gel. l-His promoted the formation of MPs gel structure with small pores and thin strands at 1 mm NaCl. These resulted in the enhanced water retention and weak gel strength of MPs in low ionic strength solution. The water-binding capacity of MPs gels formed in 1 mm NaCl containing 5 mm l-His was equivalent to that with 0.6 m NaCl. The information could offer certain theoretical foundation to apply l-His as sodium salt substitute for developing low-salt meat gelling product with high yield.