Here, we report a novel ‘double Pickering stabilization’ of W/O emulsions, where complex formation at the interface between Pickering polyphenol particles adsorbing from the oil side and WPM particles co-adsorbing from the aqueous side of the interface is investigated. The interfacial complex formation was strongly dependent on the concentration of WPM particles. At low WPM concentrations, both polyphenol crystals and WPM particles are present at the interface and the water droplets were stabilized through their synergistic action, whilst at higher concentrations, the WPM particles acted as ‘colloidal glue’ between the water droplets and polyphenol crystals, enhancing the water droplet stability for more than 90 days and prevented coalescence. Via this mechanism, addition of WPM up to 1 wt% gave a significant improvement in the stability of the W/O emulsions, allowing increasing to 20 wt% water droplet fraction. The evidence suggests that the complex was probably formed due to electrostatic attraction between oppositely-charged polyphenol Pickering particles on the oil side of the interface and WPM ‘Pickering’ particles mainly on the aqueous side of the interface. Interfacial shear viscosity measurements and monolayer (Langmuir trough) experiments at the air-water interface provided further evidence of this strengthening of the film due to the synergistic particle-particle complex formation at the interface.

There is emerging evidence on the importance of food-derived bioactive peptides to promote human health. Compared with animal derived proteins, plant proteins, in particular oilseed proteins, are considered as affordable and sustainable sources of bioactive peptides. Based on our previous bioinformatic analysis, five oilseed proteins (flaxseed, rapeseed, sunflower, sesame and soybean) were enzymatically hydrolysed using alcalase and pepsin (pH 1.3 and pH 2.1). Further, low molecular weight (Mw ​< ​3 ​kDa) fractions were generated using ultrafiltration. The protein hydrolysates and their low Mw fractions were evaluated for their in vitro antioxidant, antihypertensive and antidiabetic capabilities, in comparison with samples obtained from two dairy proteins (whey and casein). Apart from dipeptidyl-peptidase IV inhibition, significantly stronger bioactivities were detected for the low Mw fractions. In partial agreement with in silico predictions, most oilseed hydrolysates exerted comparable angiotensin-converting enzyme inhibitory capability to dairy proteins, whilst whey protein was the most promising source of dipeptidyl-peptidase IV inhibitors. Apart from alcalase-treated soybean, dairy proteins were more efficient in releasing antioxidant peptides as compared to oilseed proteins. On the other hand, soybean protein hydrolysates showed the highest α-glucosidase inhibitory activity amongst all protein sources. Overall, there was limited correlation between in silico predictions and in vitro experimental results. Nevertheless, our results indicate that oilseed proteins have potential as bioactive peptide sources, and they might therefore be suitable replacers for dairy proteins as well as good sources for development of functional foods.