Sinapic acid impacts the emulsifying properties of rapeseed proteins at acidic pH

Extensive purification of plant proteins is probably not a prerequisite for their emulsifying properties, however, details the interfacial stabilization mechanism less purified protein extracts are sufficiently known. Phenolic compounds present in can interact with proteins, inducing aggregation, impeding properties. Here, we show that when rapeseed mixture (RPM) containing 40 wt% and 6 sinapic acid used to form oil-in-water emulsions (10.0 oil) at pH 3.8 different concentrations (0.2–1.5 wt%), emulsion droplets 2.0–0.6 ?m formed large aggregates randomly attached droplet interface. By reducing content 2.5 produce concentrate (RPC) (65 proteins), smaller (0.4–0.5 ?m) same concentrations, no According our findings, both RPM- RPC-stabilized emulsions, napins primarily adsorb interface, while cruciferins secondary layer which protects against coalescence during homogenization. However, RPM, higher possibly induces aggregation cruciferins, hinders formation sufficient layer. As result, homogenization, colliding coalesce, resulting larger droplets. Our findings affects emulsification acidic pH, recommend might be necessary application food products.