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Natural plant-derived protein with excellent bioactivities has attracted much attention so a functional protein with molecular weight of 15.2 kDa was extracted from  Millettia speciosa  Champ. leaf for the first time. Under the pH of 12.0, solid-liquid ratio of 1:40 (w/v), extraction time of 2.0 h, and extraction temperature of 50 °C, the highest extracting efficiency (79.25 ± 0.78%) of the  Millettia speciosa  Champ. leaf protein (MLP) was achieved. The main structure of MLP contained β-fold and β-corner by Fourier transform infrared spectroscopy (FTIR) and Circular dichroism (CD) spectra analysis. Additionally, MLP was predominant with glutamic acid, aspartic acid, and leucine, which could be considered as a high quality natural protein. MLP showed great water holding capacity (WHC), oil absorption capacity (OAC), as well as emulsifying and foaming properties. Simultaneously, MLP exhibited considerable antioxidant activity. These results suggested that MLP could be utilised as a promising ingredient of functional foods.

Extraction and characterization of a functional protein from Millettia speciosa Champ. leaf