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

Consumers\u27 interest in functional foods has significantly increased in the past few years. Hazelnut meal, the main valuable byproduct of the hazelnut oil industry, is a rich source of proteins and bioactive peptides and thus has great potential to become a valuable functional ingredient. In this study, hazelnut protein hydrolysates obtained by a single or combined hydrolysis by Alcalase and Neutrase were mainly characterized for their physicochemical properties (SDS-PAGE, particle size distribution, Fourier-transform infrared (FTIR) spectroscopy, molecular weight distribution, etc.) and potential antiobesity effect (Free fatty acid (FFA) release inhibition), antioxidant activity (DPPH and ABTS methods), and emulsifying properties. The impact of a microfluidization pretreatment was also investigated. The combination of Alcalase with Neutrase permitted the highest degree of hydrolysis (DH; 15.57 \ub1 0.0%) of hazelnut protein isolate, which resulted in hydrolysates with the highest amount of low-molecular-weight peptides, as indicated by size exclusion chromatography (SEC) and SDS-PAGE. There was a positive correlation between the DH and the inhibition of FFA release by pancreatic lipase (PL), with a significant positive effect of microfluidization when followed by Alcalase hydrolysis. Microfluidization enhanced the emulsifying activity index (EAI) of protein isolates and hydrolysates. Low hydrolysis by Neutrase had the best effect on the EAI (84.32 \ub1 1.43 (NH) and 88.04 \ub1 2.22 m2/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 \ub1 1.06% DPPH and 98.31 \ub1 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

Interactions between Hazelnut (Corylus avellana L.) Protein and Phenolics and In Vitro Gastrointestinal Digestibility

In this study, we investigated the formation of protein–phenolic complexes from dephenolized hazelnut meal protein isolates (dHPI) and hazelnut skin phenolic extracts (HSE) and their effects on the bioaccessibility of both hazelnut proteins and phenolics. The dHPI–HSE complexes were of considerable size and were dependent on HSE concentration due to aggregation. Although catechin was the main component of HSE, it did not cause aggregation, except for a slight rise in particle size. According to fluorescence quenching, the hazelnut protein–phenolic extract complex had a linear Stern–Volmer plot expressing static quenching between 0–0.5 mM concentration; the interaction was mainly dependent on hydrogen bonding and van der Waals forces (ΔH < 0 and ΔS < 0), and the reaction was spontaneous (ΔG < 0). According to Fourier transform infrared (FTIR) spectroscopy results, higher phenolic extract concentration caused an increase in irregular structures in hazelnut protein, while the lowest catechin and phenolic concentration altered the regular structure. Skin extracts did not alter the digestibility of dephenolized proteins, but dephenolization reduced the degree of hydrolysis by pancreatin. The formation of the protein–phenolic complex had a beneficial effect on the bioaccessibility of hazelnut skin phenols, predominantly those on the galloylated form of the catechins, such as gallocatechin gallate and epigallocatechin gallate. Thus, the bioaccessibility and antioxidant activity analysis results showed that protein–phenolic complexes obtained from hazelnut meal and skin may promote the transition of phenolic compounds from the gastrointestinal tract without degradation