Effect of malondialdehyde oxidation on structure and physicochemical properties of amandin

Oil, accounting for 45% of almonds, is easily oxidised and can further induce the protein oxidation to reduce their quality. Structure and physicochemical properties of amandin, the main water-soluble protein in almonds, inducing oxidation by malondialdehyde (MDA) were investigated. The results showed that the content of carbonyl group increased from 5.23 to 33.25 nmol mg(-1) of protein with the increase in MDA concentration (P < 0.05). However, the sulphydryl content, surface hydrophobicity, particle size and the absolute value of zeta-potential first increased and then decreased. Fourier-transformed infrared spectroscopy (FT-IR) confirmed that the structure of amandin changed from order to disorder. Fluorescence spectroscopic analysis revealed that mild oxidation (0-0.1 mmol L-1 MDA) exposed hydrophobic groups of the protein. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that protein oxidation promoted crosslinking between protein molecules. Furthermore, protein oxidation markedly declined the total amino acid content of amandin (P < 0.05). In conclusion, MDA oxidation changed the structure and amino acid content of amandin, and caused the protein aggregate and crosslink through hydrophobic interaction and electrostatic interaction.