The solubility and conformational characteristics of porcine myosin as affected by the presence of l-lysine and l-histidine. (1st March 2015)

• Record Type: Journal Article
• Authors: Guo, X.Y.; Peng, Z.Q.; Zhang, Y.W.; Liu, B.; Cui, Y.Q.
• Is Part Of: Food chemistry. Volume 170(2015)
• Page Start: 212
• Page End: 217
• Publication Date: 2015-03-01
• Subjects: Myosin -- l-lys -- l-his -- Solubility -- Conformation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2014.08.045
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: l -his andl -lys cause the transformation of secondary structures of porcine myosin. R-SH and hydrophobic groups are exposed in the presence ofl -his andl -lys. l -his andl -lys increase the solubility of porcine myosin at all ionic strengths. l -lys contributes more to solubility thanl -his due to more loss of α-helix. Abstract: The influence ofl -lys andl -his on the solubility, surface hydrophobicity, sulphydryl content and conformational characteristics of porcine myosin solubilised in high (0.6 M), physiological (0.15 M) and low (1 mM) ionic strength solutions were explored. The solubility of myosin was increased in the presence ofl -his and/orl -lys in all ionic strength solutions used. The presence ofl -his andl -lys caused increases in the surface hydrophobicity and reactive sulphydryl content ( p < 0.05). Circular dichroism revealed a significant decrease of α-helical content with an increase of random coils, β-turns and β-sheets in the presence ofl -his and/orl -lys. These results demonstrate that the introduction ofl -lys andl -his causes the unfolding of myosin, resulting in loss of α-helical structure, which is followed by increases in random coils, β-turns and β-sheets, which exposes buried hydrophobic and sulphydryl groups to the myosin surface, ultimately increasing the solubility of porcine myosin.