Effect of sodium bicarbonate and sodium chloride on aggregation and conformation of pork myofibrillar protein. (15th July 2021)

• Record Type: Journal Article
• Authors: Li, Yan-ping; Zhang, Xue-hua; Lu, Fei; Kang, Zhuang-Li
• Is Part Of: Food chemistry. Volume 350(2021)
• Publication Date: 2021-07-15
• Subjects: Sodium bicarbonate -- Sodium chloride -- Hydrophobic -- Myofibrillar protein -- Ca2+-ATPase; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.129233
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: Partial replacement of sodium chloride by sodium bicarbonate increased pH, active sulfhydryl, and surface hydrophobic. Partial replacement of sodium chloride by sodium bicarbonate decreased turbidity, particle size, and Ca 2+ -ATPase activity. Partial replacement of sodium chloride by sodium bicarbonate unfolded and dissociated myofibrillar protein. Adding sodium bicarbonate led the myofibrillar protein to undergo denaturation easily. Abstract: To investigate the effect of sodium bicarbonate instead of sodium chloride, the changes in pH, turbidity, aggregation, and conformation of myofibrillar protein solution with various amounts of sodium chloride and sodium bicarbonate were studied. When the sodium bicarbonate was increased from 0% to 0.4%, accompanied by the sodium chloride being decreased from 2.0% to 0.8%, the pH increased about 1.20 unites; the absolute values of the Zeta potential, active sulfhydryl, and surface hydrophobicity increased significantly ( p < 0.05); and the turbidity, particle size, and Ca 2+ -ATPase activity decreased significantly ( p < 0.05). In addition, the Mg 2+ -ATPase activity was not significantly different ( p > 0.05) when increasing sodium bicarbonate, implying that sodium bicarbonate did not affect the actin. Overall, the results indicated that an increase in sodium bicarbonate could improve solubility, expose more hydrophobic residues and sulfhydryl groups, and induce Ca 2+ -ATPase inactivation and protein unfolding, leading the myofibrillar protein to denaturation easily.