Enhancement of foaming performance of hempseed protein by limited enzymatic hydrolysis: From the viewpoint of the structural and interfacial rheological attributes

Effects of limited enzymolysis by Alcalase and Protamex on the foaming performance of hempseed protein (HPI) and its correlation with structural and interfacial rheological characteristics were investigated. Proteolysis induced a conformational shift from alpha-helix and beta-sheet to random coil, indicating enhanced molecular flexibility. The surface hydrophobicity of Alcalase hydrolysates encountered an initial increase (5 min) followed by a sharp drop with prolonged hydrolysis, whereas Protamex showed minimal effects. Both proteases reduced total sulfhydryl content and caused a redshift in intrinsic fluorescence, particularly Alcalase. The specific cleavage pattern of Alcalase generated peptides with pronouncedly higher solubility (up to 47.0 %) relative to Protamex. The flexible conformation and increased solubility induced by moderate proteolysis, notably with Alcalase, facilitated viscoelastic interfacial membranes with consolidated intermolecular interactions, consequently contributing to more homogeneous and smaller bubble structures. Optimal foaming capacity (95.0 %) and foam stability (90.9 %) were achieved with Alcalase for 20 min and 5 min, respectively.