Abstract: In this paper, the conjugates of lentil protein isolate (LPI) and gum Arabic (GA) were prepared by the wet-heating Maillard reaction, and their structures were characterized. When the mass ratio of LPI to GA was larger than 1:1, the degree of the Maillard reaction increased with the increase of GA proportion. When the mass ratio was less than 1:1, the degree of the Maillard reaction decreased with the increase of GA proportion. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) spectra results indicated that covalent bonds were formed between LPI and GA. Endogenous fluorescence spectra and surface hydrophobicity analysis confirmed that the introduction of GA changed the conformation of natural LPI and enhanced its surface hydrophobicity. X-ray diffraction (XRD) and scanning electron microscope (SEM) results showed that the crystallinity of the LPI-GA conjugates was reduced by the Maillard reaction, resulting in a loose and brittle sheet-like microstructure. This study provides a theoretical basis for improving the high-value utilization of LPI.
Keywords: lentil protein isolate(LPI); gum Arabic(GA); Maillard reaction; conjugates
合肥工业大学学报自科版