Functional and physicochemical characterization of Vicia cracca protein: A promising novel plant protein source

With the growing global demand for alternative protein sources, the identification and characterization of alternative plant proteins have become essential. In this study, the thermal and physicochemical characteristics, functional properties, viscosity behavior, and proximate composition of protein isolates obtained from Vicia cracca seeds (VCPI) were investigated using an alkaline extraction method. Results indicated that VCPI contained 87.84% protein, 18.61% glutamic acid and 12.87% aspartic acid. In addition, VCPI exhibited a surface hydrophobicity measuring 7028.90, contained 16.81 ± 0.65 μmol/g of free sulfhydryl groups, had an average size of 150.30 nm (hydrodynamic R), a particle polydispersity index of 0.43, and a surface charge measuring -33.43 mV. Additionally, VCPI demonstrated remarkable solubility, foaming, emulsifying, and rheological properties, along with a high-water adsorption capacity of 204.29%. Moreover, VCPI showed pH-dependent protein solubility. The protein isolate also had two denaturation temperatures of 63.64 and 127.64 °C. It also had an L * value of 84.80. Scanning electron microscopy revealed a rough surface. Overall, the results suggest that VCPI could serve as an excellent protein source with exceptional functional properties. • VCPI contains 87.84% protein, making it a rich protein source. • VCPI shows excellent solubility, foaming, emulsifying, and rheological properties. • VCPI has a higher denaturation temperature, suitable for heat-induced interactions and process design. • VCPI’s amino acid profile meets recommended levels for a healthy diet, with aspartic acid (Asp) and glutamic acid (Glu) being the major amino acids.