Physicochemical and stability analysis of mung bean protein hydrolysates with lipid peroxidation inhibition.

This study investigated mung bean protein hydrolysates (MBPH) produced using neutral protease, examining their physicochemical properties, stability, and lipid peroxidation inhibition capabilities. The research revealed that MBPH molecular weight ranged from 17 to 26 kDa and perform various functions, including catalytic, nutrient storage, and binding. Stability assessments showed that MBPH are stable at 45 °C and pH of 7.5 but are light-sensitive and unstable in solution or when combined with sugars. Additionally, increased concentrations of digestive enzymes reduce MBPH stability. Antioxidant tests in vitro and in Caenorhabditis elegans confirmed MBPH's ability to neutralizing radicals, enhance antioxidant enzyme activities, and reduce lipid peroxidation, thereby protecting against oxidative damage. Furthermore, in vivo experiments showed that MBPH extend the lifespan of worms and reduced their body lipid content, indicating potential benefits in mitigating cholesterol-related damage. This research demonstrates the potential of MBPH in inhibiting lipid peroxidation.