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

Abstract

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.

Effect of bamboo shoot dietary fiber on gel properties, microstructure and water distribution of pork meat batters

“…The gel strength of heated pork batters was determined by a TA-XT2i Plus texture analyzer equipped with a 5.0 mm diameter aluminous cylindrical probe as described by Chen et al [26] with slight modifications. Ten heated pork batter samples (20.0 mm height) for each formulation were compressed using a trigger-type button with a 2 mm/s pretest speed, a 1.0 mm/s test speed, a 1.0 mm/s posttest speed, 10 mm distance and 5 g trigger force.…”

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

“…Theoretically, both Lys and Arg may have significant but different influences on chicken myosin gel. To date, a few papers have reported on the effects of histidine on the thermal gelling properties of the myosin system [16,17] and the effects of Arg on actomyosin [18] or the SSMP system. [19] However, information is lacking regarding the effects of Lys or Arg on the thermal gelling properties of the myosin system.…”

Effect of pH-values on gelation properties of myosin extracted from high-pressure treated pre-rigor rabbit muscle

“…NMR relaxation measurements were performed according to the method described by Chen et al (2016) with slight modifications. The gel sample (2.0 ± 0.1 g) was placed in a glass tube (15 mm in diameter) and inserted into the probe of a PQ001 Niumag Pulsed NMR analyzer (Niumag Electric Corporation, Shanghai, China).…”