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Covalent modification of (+)-catechin to improve the physicochemical, rheological, and oxidative stability properties of rice bran protein emulsion

  • Dan Li
  • , Rongchun Wang
  • , Ying Ma*
  • , Dianyu Yu
  • *Corresponding author for this work
  • School of Chemistry and Chemical Engineering, Harbin Institute of Technology
  • Northeast Agricultural University

Research output: Contribution to journalArticlepeer-review

Abstract

The aim of this study is the effects of (+)-catechin (CC) covalent cross-linking (CCCI) (0.05–0.25 %, w/v) on the physicochemical properties, rheological properties, and oxidative stability of rice bran protein (RBP) emulsion. Analysis of particle size, ζ-potential, circular dichroism, fluorescence spectroscopy, surface hydrophobicity, and emulsifying properties demonstrated that a concentration of 0.15 % (w/v) CCCI facilitated protein structure unfolding, resulting in reduced particle size, enhanced electrostatic repulsion, and improved emulsion stability. Moreover, the covalent complexes of RBP-0.15 %CC (w/v) exhibited increased viscosity and shear stress, reflected by the highest G′ and G″ values, ultimately enhancing the oxidative stability. Furthermore, analysis using atomic force microscopy and confocal laser scanning microscopy revealed that the RBP-0.15 %CC complexes exhibited the smallest particle size (164 nm) and displayed greater homogeneity. An increase in CC concentration to 0.25 % (w/v) resulted in a higher emulsion aggregation. The emulsions stabilized by CCCI exhibited superior rheological properties and enhanced oxidation stability compared to the control. In conclusion, an appropriate amount of CC can enhance the rheology and oxidation stability of the RBP emulsion, while CCCI treatment holds potential for expanding the utility of RBP in various applications.

Original languageEnglish
Article number126003
JournalInternational Journal of Biological Macromolecules
Volume249
DOIs
StatePublished - 30 Sep 2023
Externally publishedYes

Keywords

  • (+)-Catechin
  • Covalent interaction
  • Lipid oxidation
  • Physicochemical stability
  • Rheological properties
  • Rice bran protein

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