Combined Neutrase–Alcalase Protein Hydrolysates from Hazelnut Meal, a Potential Functional Food Ingredient

/g (MFNH)), while a negative correlation between the emulsifying stability index (ESI) and the DH was observed. Again, the combined Alcalase-Neutrase hydrolysates displayed the highest radical scavenging activities (96.63 ± 1.06% DPPH and 98.31 ± 0.46% ABTS). FTIR results showed that the application of microfluidization caused the unfolding of the protein structure. The individual or combined application of the Alcalase and Neutrase enzymes caused a switch from the β-sheet organization of the proteins to α-helix structures. In conclusion, hazelnut meal may be a good source of bioactive and functional peptides. The control of its enzymatic hydrolysis, together with an appropriate pretreatment such as microfluidization, may be crucial to achieve the best suitable activity.