Effects of Heat Treatment on Physicochemical Properties of Moringa oleifera Lam. Leaf Protein

M. oleiferaleaves represent a novel and nutritious food. Prior research has demonstrated thatM. oleiferaleaves can elicit allergic responses in BALB/c mice. Based on these findings, further studies were conducted to investigate the effects of heat treatment on the allergenicity, particle size, zeta potential, total sulfhydryl (TSH) content, hydrophilicity and hydrophobicity, ultraviolet spectrum, and intrinsic fluorescence spectrum ofM. oleiferaleaf protein. Additionally, in vitro digestion experiments were carried out to gain further insights into the protein’s behavior under these conditions. The experiment simulated the alterations inM. oleiferaleaf protein during the processes of cooking and digestion. The findings of this experiment can provide certain guidance for the processing ofM. oleiferaleaf products. The hydrophilicity, hydrophobicity, transmembrane region, antigen index, calcium binding site, spatial structure, and homology ofM. oleiferaleaf fructose 1,6 bisphosphate aldolase (FBA) were simulated and calculated based on the amino acid sequence of the 36 kDa allergen. These parameters collectively serve to indicate the allergenic activity of the peptide. The findings of the analysis align with the outcomes of the sensitization experiments, suggesting that the FBA ofM. oleiferaleaves is indeed consistent. In conjunction with the heat treatment experiments, this research can inform the preparation ofM. oleiferaleaf foods and provide a foundation for further investigation intoM. oleiferaleaf allergens.