RESUMEN
Cold press manufacture of black cumin (BC) oil leads to the formation of BC press cakes that contain significant amounts of protein. Here, an attempt was made to enhance the functionality of BC protein concentrates obtained from cakes based on Maillard conjugation using 3 different of carbohydrates. Molecular weight distribution of the conjugates was determined via electrophoretic techniques. The extent of carbohydrate binding was measured by RP-HPLC-RID. Surface activity and elasticity was studied using drop shape tensiometry. The extent of glucose binding accounted for up to 85% for a protein:glucose ratio of 1:2. Foaming capabilities were moderately enhanced due to Maillard conjugation in the absence of solvent extraction, while due to solvent induced partial denaturation, further enhancement of foaming performance took place. Furthermore, sugar binding capabilities were enhanced upon solvent treatment, while surface pressure and foaming capacity were not necessarily improved. Adsorption rate at the air-water surface and dilational elasticity was highly dependent on molecular size of reacting sugars. In addition, oil remaining in the samples also had a bearing on the extent of Maillard conjugation. Consequently, tailoring of processing conditions could enhance foaming characteristics of BC proteins and ensure their utilization in food foams and other food dispersions.
RESUMEN
Cold press technology generates high quality value-added oil products along with highly stable oilseed cakes. Hazelnut cakes are characterized by high protein concentrations that can be industrially valorized. Here, using an aqueous extraction scheme along with enzymatic proteolysis and FPLC (fast protein liquid chromatography)-based fractionation, a variety of hazelnut peptide fractions with varying bioactive properties were manufactured and their sequences were determined based on mass spectrometry. DPP-IV inhibitory attributes were determined based on an in vitro DPP-IV assay and in silico techniques were administered for for the analysis of overall bioactive potential and DPP-IV inhibitory characteristics of peptides. Based on these investigations, 256 peptides were identified in 81 different fractions. The majority of fractions were characterized with low to moderate DPP-IV inhibitory activity possibly due to their dilute nature. Some hazelnut peptides were characterized by comparable IC50 values as the positive control (Diprotin-A). The most influential 7 peptides were shown to generate higher docking scores than the control. The main interaction mechanism between hazelnut peptides and DPP-IV possibly depended on hydrophobic interactions. While further concentration could enhance the DPP-IV inhibitory potential of hazelnut peptides, hazelnut cakes represent a sustainable resource of potentially antidiabetic peptides.