Phosphorylation of Myofibrillar Proteins and the Effect of Polyphenols Synergistic Phosphorylation on Proteinaceous Gel Properties
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    Abstract:

    In this paper, chicken breast as raw material, myofibrillar proteins were phosphorylated with sodium tripoly phosphate (STP). On the basis of single-factor investigation, response surface methodology was employed to establish optimum conditions for phosphorylation, and discussed the effect of polyphenols (chlorogenic acid and gallic acid) synergistic phosphorylation on proteinaceous gel properties. The results showed that the optimal conditions of myofibrillar protein phosphorylation were pH 7.52, protein concentration 15.36 mg/mL, NaCl concentration 0.75 mol/L, reaction time 2 h, and STP content 3.40%. Under this condition, the degree of phosphorylation was 99.001 mg/g. The degree of protein phosphorylation obtained by simulating the actual processing of meat products was close to the experimental results, which proved the feasibility of phosphorylation. After phosphorylation, the gelling elasticity, whiteness and water retention of myofibrillar protein were increased varying degrees, which explained that phosphorylation can improve the gel properties of proteins. In addition, compared to chlorogenic acid, gallic acid had more significant effects on various aspects of gel properties; as the concentration of polyphenols increased, the gel hardness first increased and then decreased; the gel elasticity didn't change significantly. The gel whiteness first decreased and then increased with the increasing of chlorogenic acid concentration, and decreased with the increasing of gallic acid concentration. The water retention of the gel gradually increased with the concentration of polyphenols increasing.

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  • Online: July 31,2020
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