Lentil protein: impact of different extraction methods on structural and functional properties

Plant proteins with improved solubility, foaming, and emulsifying properties are required to meet the demand for plant-based foods. This study evaluated the influence of alkaline extraction combined with enzyme- and ultrasound-assisted extraction on lentil protein structure and functionality. Enzyme- and ultrasound-assisted extractions were not capable of increasing the protein yield compared to alkaline extraction alone. However, the purity of isolated protein was dependent on the extraction process, ranging from 82.7% to 90%. Although the molecular mass, zeta potential profiles, and denaturation temperature were not dependent on the extraction method, the enthalpy of denaturation for protein obtained solely by alkaline extraction was significantly lower than that for assisted processes, indicating that protein denaturation is caused by an alkaline process. Changes in protein structure were also suggested by solubility analyses that showed that lentil proteins obtained by enzyme-assisted and ultrasound-assisted extraction have better solubility at pH 7 when compared to alkaline extraction alone. The surface activity of lentil protein was evidenced by interfacial and surface analysis, and it was influenced by the extraction process applied. We demonstrated that combining alkaline extraction with assisted processes, especially ultrasound technology, results in concentrates/isolates with higher solubility as compared to ones obtained solely by the traditional alkaline method, even though the choice of extraction method should depend on the desired functionality. •Proteins from lentil were efficiently recovered by alkaline extraction.•Lentil protein solubility was improved by ultrasound and enzyme extraction.•Lentil protein surface activity was dependent on the extraction process.•Foaming properties were improved by ultrasound extraction.•Emulsifying properties were not influenced by the extraction process. Ultrasound-assisted; Enzyme-assisted; Viscozyme L; Plant protein; Functional properties.