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

Abstract

SummaryThe 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.