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

• Published in: International journal of food science & technology 2016-05, Vol.51 (5), p.1195-1203
• Main Authors: Chen, Xing, Li, Yong, Zhou, Ruiyun, Liu, Zhaiming, Lu, Fengzhi, Lin, Huang, Xu, Xinglian, Zhou, Guanghong
• Format: Article
• Language: English
• Subjects: Breast; Chickens; Equivalence; Food science; Gelation; Gelation properties; l-histidine; low-salt meat products; Meat; myofibrillar proteins; Poultry; Proteins; sodium reduction; Solubility; Strength; water-binding capacity
• ISSN: 0950-5423; 1365-2621
• DOI: 10.1111/ijfs.13086

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. Effects of 5 mm l‐histidine on the gel properties of chicken breast myofibrillar proteins in low ionic strength solution.