l‐histidine improves water retention of heat‐induced gel of chicken breast myofibrillar proteins in low ionic strength solution

Summary The effects of 5 m m l ‐histidine ( l ‐His) on water‐binding capacity, gel strength, thermal gelling properties of chicken breast myofibrillar proteins (MPs) in 1 m m 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 m m NaCl. l ‐His at 1 m m 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 m m 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 m m NaCl containing 5 m m 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.