Effect of Na+ and Ca2+on the texture, structure and microstructure of composite protein gel of mung bean protein and wheat gluten

To investigate the change of ionic strength on the gel characteristics during the processing of mung bean protein -based foods, the effects of NaCl and CaCl2 at different concentrations (0-0.005 g/mL) on the properties of mung bean protein (MBP) and wheat gluten (WG) composite protein gel were studied. The results showed that low concentration (0.001-0.002 g/mL) could significantly improve the water holding capacity (WHC), storage modulus (G') and texture properties of composite protein gel (MBP/WG), while the surface hydrophobicity (H0) and solubility were significantly decreased (P < 0.05). With the increase of ion concentration, the secondary structures of MBP/WG shifted from & alpha;-helix to & beta;-sheet, and the fluorescence spectra also showed fluorescence quenching phenomenon. By analyzing the intermolecular forces of MBP/WG, it was found that with the addition of salt ions, the hydrogen bonds was weakened and the electrostatic interactions, hydrophobic interactions and disulfide bonds were enhanced, which in turn the aggregation behavior of MBP/WG composite protein gel was affected and larger aggregates between the proteins were formed. It could be also demonstrated that the gel network was denser due to the addition of these large aggregates, thus the gel properties of MBP/WG was improved. However, too many salt ions could disrupt the stable network structure of protein gel. This study can provide theoretical support to expand the development of new mung bean protein products.