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

M. oleifera leaves represent a novel and nutritious food. Prior research has demonstrated that M. oleifera leaves 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 of M. oleifera leaf 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 in M. oleifera leaf protein during the processes of cooking and digestion. The findings of this experiment can provide certain guidance for the processing of M. oleifera leaf products. The hydrophilicity, hydrophobicity, transmembrane region, antigen index, calcium binding site, spatial structure, and homology of M. oleifera leaf 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 of M. oleifera leaves is indeed consistent. In conjunction with the heat treatment experiments, this research can inform the preparation of M. oleifera leaf foods and provide a foundation for further investigation into M. oleifera leaf allergens.