Laccase-mediated Cross-linking of Rice Protein with Ferulic Acid: Changes in Structural Properties and Antioxidant Activity
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Abstract:
The enzymatic cross-linking of rice protein (RP) and ferulic acid (FA) and the antioxidant activity of the resultant product in the aqueous phase and emulsion were studied, and the FA content was investigated by high performance liquid chromatography (HPLC). Changes in the structural properties of RP were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), ultraviolet (UV) spectroscopy, Fourier transformed infrared (FT-IR) spectroscopy, and scanning electron microscopy. HPLC results showed that the FA easily underwent laccase-catalyzed oxidation, and the oxidation product could react with the subunits of RP, resulting in an increase of RP protein molecular weight. With increasing FA concentration, the absorbance band between 300 and 350 nm in the UV/visible spectra of RP gradually increased, and the cross-linked products had an orange-yellow color, indicating that the oxidation products bound covalently to the free amino groups of RP. After the enzymatic cross-linking of RP and FA, the secondary structure of RP changed, the contents of β-turn and α-helix were reduced by 13% and 2%, respectively, the contents of random coil and β-sheet were increased by 11% and 4%, respectively, and the microstructure of RP became loosened from the aggregated state. 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) free radical scavenging abilities of the RP-FA cross-linked product were increased from 32.31% to 71.43% and from 3.34 % to 77.61%, respectively, compared to those of RP. RP-FA cross-linked product could significantly reduce the level of hydroperoxide, 2-thiobarbituric acid reactive substances (TBARS), and hexanal in the emulsion, suggesting that cross-linking of RP can effectively enhance the antioxidant activity of RP.
