Physicochemical and chemical properties of mung bean protein isolate affected by the isolation procedure

Christina Wintersohle, Inola Kracke, Laura Melanie Ignatzy, Lara Etzbach, Ute Schweiggert-Weisz

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The effects of different mung bean protein isolation methods on the chemical composition, the physicochemical properties, and selected antinutritional factors of mung bean protein isolates were investigated. Six protein isolates were prepared by isoelectric precipitation at different extraction pH levels (pH 8 and 9), by micellization, and by hybrid isolation at varying salt concentrations (0.25 M, 0.50 M, 0.75 M). The extraction conditions affected the amount of antinutritive compounds of the isolates. Compared to mung bean flour, micellization reduced phytic acid content by approximately 48% and trypsin inhibitor activity by around 88%. The remaining phytic acid concentration of the isolates influenced their re-solubility, particularly under acidic conditions. The protein isolates exhibited significant differences in surface hydrophobicity and thermal characteristics, indicating structural modifications caused by the extraction methods. Micellization and extraction at pH 8 were identified as mildest isolation methods, as evidenced by the highest enthalpy values. SDS-PAGE analysis demonstrated an enrichment of globulins and comparable protein profiles among the isolates, suggesting that the observed differences arise from conformational changes rather than variations in protein composition. The product yield in protein extraction from mung beans ranged from 8% to 19%, emphasizing the importance of enhancing overall extraction efficiency or exploring the utilization of by-products obtained during the protein isolation process.

Original languageEnglish
Article number100582
JournalCurrent Research in Food Science
StatePublished - Jan 2023
Externally publishedYes


  • FT-IR
  • Isoelectric precipitation
  • Micellization
  • Phytic acid
  • Protein solubility
  • Protein yield


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