Enzymatic Low-Molecular-Weight Modification of Mung Bean Protein Isolate: Effects on Physicochemical Characteristics and Cosmetic Bioactivities
Jiseon Lee, Seonghyeon Lee, Daewoo Lee, Kilteak Hwang, Hyejin Hong, Soyoung Shin, Hyo Tae KimIn this study, we investigated the effects of enzymatic low-molecular-weight modification on the physicochemical characteristics and cosmetic-related bioactivities of mung bean protein isolate. Mung bean protein isolate (MBPI) was prepared by alkaline extraction and isoelectric precipitation, followed by sequential treatment with Viscozyme L and Protana Prime, and centrifugal filtration was then performed to obtain a low-molecular-weight fraction (LMBPI). Among the tested enzymatic treatment conditions, the selected condition produced the lowest mean particle size (160.09 ± 2.24 nm). The resulting hydrolysate showed a solubility of 93.98 ± 0.43%, compared with 89.08 ± 1.49% for untreated MBPI. SDS-PAGE and molecular weight distribution analyses showed that enzymatic treatment decreased the proportion of high-molecular-weight proteins and increased the low-molecular-weight fractions, with the 1–5 kDa fraction reaching 60% after centrifugal filtration. Compared with MBPI, LMBPI exhibited greater DPPH and ABTS radical scavenging activities and more effectively reduced nitric oxide and prostaglandin E2 production in lipopolysaccharide-stimulated RAW264.7 cells. LMBPI also showed higher tyrosinase and elastase inhibitory activities and reduced α-MSH-induced melanin production in B16F10 cells and UVA-induced matrix metalloproteinase-1 production in human dermal fibroblasts. These results indicate that enzymatic low-molecular-weight modification generated a smaller, lower-molecular-weight mung bean protein fraction with greater antioxidant, anti-inflammatory, anti-melanogenic, and anti-wrinkle-related activities than untreated MBPI, suggesting the potential of LMBPI as a multifunctional plant-derived cosmetic ingredient.