Solubility of Chicken Breast Muscle Proteins in Solutions of Low Ionic Strength

Abstract

Essentially all of the proteins of chicken breast muscle were soluble in sodium chloride solutions of physiological ionic strength or less and neutral pH. However, there was a critical order of treatment necessary to accomplish this. After removal of those proteins solubilized by homogenizing the tissue 1:10 (w/v) in water, it was necessary to solubilize a fraction of the remaining proteins in moderate concentrations (25-150 mM) of sodium chloride at neutral pH before the remaining proteins could be solubilized in water. Solubilization of chicken breast muscle proteins in water could be prevented or reversed by salt solutions of low concentration, suggesting that most of the solubility was not directly caused by proteolysis. SDS-polyacrylamide gel electrophoresis indicated that removal of specific peptides by moderate concentrations of sodium chloride at neutral pH was correlated with removal of the restriction on the water solubility of the remaining proteins.

The solubility and conformational characteristics of porcine myosin as affected by the presence of l-lysine and l-histidine

“…Takai et al (2013) showed that the marginal solubilisation effect of lys might be because of the strong tendency of myosin to self-associate into filaments at low NaCl concentration, and a specific interaction between lys and myosin may disrupt the electrostatic interactions and prevent filament formation. Krishnamurthy et al (1996) suggested that L-his was important for neutralising the low ionic strength solution and did not have a specific effect on the solubilisation of myofibrillar proteins. Contrary to the Krishnamurthy et al (1996) study, Hayakawa et al (2009 found that L-his directly affected the solubility of myosin in a low (1 mM) ionic strength solution rather than observing a pH effect.…”

“…Krishnamurthy et al (1996) suggested that L-his was important for neutralising the low ionic strength solution and did not have a specific effect on the solubilisation of myofibrillar proteins. Contrary to the Krishnamurthy et al (1996) study, Hayakawa et al (2009 found that L-his directly affected the solubility of myosin in a low (1 mM) ionic strength solution rather than observing a pH effect. Further studies showed that possible reason for this was because of elongation of LMM region, contributing to myosin filament weakening and the dissociation of myosin in a low ionic strength solution (Hayakawa et al, 2010).…”

“…This may be due to the effect of salts disrupting the electrostatic interactions through both non-specific binding (Debye-Hückel) and through specific ion binding to the protein (Goto, Takahashi, & Fink, 1990). Contrary to Krishnamurthy et al (1996) and Hayakawa et al (2009), we hypothesise that the mechanism of solubility enhancement by the amino acids is that L-his and L-lys cations are able of binding negative charged residues of myosin through electrostatic interaction, thereby disrupting the intra and inter molecular ionic linkages, which causes transformation of the myosin conformation, resulting in a loss of a-helical structure and the exposure of hydrophobic groups and masked SH groups to the surface. Subsequently, the depolymerisation of the myosin filament is induced, ultimately increasing the solubility of myosin.…”

“…Chicken breast (Krishnamurthy et al, 1996) and mackerel light muscles (Feng & Hultin, 1997) were also solubilised in a low ionic strength solution. To solubilise chicken breast proteins in a low ionic strength solution, washing with a sodium chloride solution buffered with L-his and dialysis against water were necessary.…”

Nutritional Quality and Physical Characteristics of Soluble Proteins Recovered from Silver Carp

“…Krishnamurthy et al. () reported CaCl 2 solutions of low ionic strength provided and inhibitory effect of protein solubility. However, as ionic strength increased, protein solubility returned to levels similar to what was observed in NaCl solutions (Krishnamurthy et al., ).…”