4.7 Article

Phase behavior, thermodynamic and rheological properties of ovalbumin/ dextran sulfate: Effect of biopolymer ratio and salt concentration

期刊

FOOD HYDROCOLLOIDS
卷 118, 期 -, 页码 -

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ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2021.106777

关键词

Ovalbumin; Dextran sulfate; Electrostatic interaction; Isothermal titration calorimetry; Rheology

资金

  1. Jilin Scientific and Technological Development Program [20190301015NY]
  2. Fundamental Research Funds fo the Central Universities

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The complexation between ovalbumin (OVA) and highly charged dextran sulfate (DS) is mainly driven by strong electrostatic interactions, with the addition of salt having diverse effects on coacervate formation. Isothermal titration calorimetry (ITC) results show that DS binds to native OVA through electrostatic forces, forming coacervates with high viscoelasticity.
The complexation between ovalbumin (OVA) and highly charged dextran sulfate (DS) was investigated employing phase behavior, zeta potential, confocal laser scanning microscope (CLSM), isothermal titration calorimetry (ITC) measurement, and dynamic rheometer analysis. The critical boundary pH values (pHc, pH?1, pHmax) were strongly dependent on the biopolymer ratio and salt concentration. Results of the phase diagram and zeta potential showed that the formation of complexes was mainly driven by strong electrostatic interactions. As the increase of the OVA/DS ratio, the critical pH values shifted to higher values. However, the addition of NaCl has a diverse effect, lower salt concentration (CNaCl <100 mM) promoted the formation of OVA/DS coacervates, while higher salt concentration (CNaCl ? 100 mM) suppress the formation of coacervates due to the shielding effect. The ITC results revealed that DS does bind to native form of OVA at pH 7.0 through the electrostatic forces and it was a spontaneous exothermic process (?G < 0, ?H < 0). Additionally, much higher viscoelasticity (G?&G?) for all OVA/DS coacervates indicates that the formation of a highly interconnected gellike structure. The maximum viscoelasticity was shown at an OVA/DS ratio of 10:1 with 50 mM NaCl. On the other hand, the addition of salt decreased the gel transition temperature of OVA thus promote its aggregation in the mixing system. Our work provides important insight for understanding the interaction between sulfated polysaccharide with egg white protein.

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