Study on Protein Structures of Eight Mung Bean Varieties and Freeze-Thaw Stability of Protein-Stabilized Emulsions.

ABSTRACT: 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

SUBMITTER: Sun H 

PROVIDER: S-EPMC9655322 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature