In order to evaluate the freeze-thaw stability of mung bean protein isolate (MPI)-stabilized emulsions and its relationship with protein structure, proteins of eight mung bean varieties were compared. The results revealed that MPIs prepared from all eight varieties were mainly composed of five subunit bands, with albumin and globulin content ranges of 188.4-310.3 and 301.1-492.7 mg/g total protein, respectively. Protein structural analysis revealed that random coil structure (32.34-33.51%) accounted for greater than 30% of MPI secondary structure. Meanwhile, analysis of protein properties revealed emulsifying activity index (EAI), emulsifying stability index (ESI) and flexibility value ranges of 6.735-8.598 m2/g, 20.13-34.25% and 0.125-0.182, respectively. Measurements of freeze-thaw stability of MPI emulsions demonstrated that exposures of emulsions to multiple freeze-thaw cycles resulted in significantly different emulsion creaming index, oiling-off, particle size and zeta potential values for the various emulsions. Moreover, the stabilities of all eight protein emulsions decreased with each freeze-thaw cycle, as demonstrated using optical micrographs. The correlation analysis method was used to study the correlation between the original structures, emulsifying properties of proteins and the freeze-thaw stability of MPI emulsions. Correlation analysis results revealed significant relationships between albumin content, subunit bands with a molecular weight of 26.9 kDa and emulsifying properties were significantly related to the freeze-thaw stability of MPI emulsion. Thus, by determining these indicator values, we can predict the freeze-thaw stability of MPI-stabilized emulsions.
Keywords: albumin and globulin content; circular dichroism; emulsion parameters; flexibility measurement; fourier-transform infrared spectroscopy; freeze-thaw stability; functional properties; mung bean protein isolate; protein structure.