Steering protein and lipid digestibility by oleogelation with protein aerogels.

The aim of the present work was to assess the effect of an innovative oleogelation strategy, the aerogel-template approach, on protein and lipid digestibility. Whey protein isolate (WP) was converted into aerogel particles via supercritical CO2 drying. Oleogels were then prepared by absorption of sunflower (SO) or flaxseed (FLX) oil (80%, w/w) into the aerogel particle template and subjected to in vitro digestion. WP aerogel-templated oleogels showed a specific destructuring behaviour during digestion. Confocal micrographs clearly demonstrated that the original oleogel structure was lost at the gastric level, with the release of oil droplets smaller (D32 < 10 µm) than those observed in the case of the unstructured oils (D32 > 30 µm), stabilised by undigested aerogel proteins. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and bicinchoninic acid (BCA) assay confirmed that aerogelation reduced the gastric proteolysis of WP from nearly 100% to 70%. The digestion of the SO oleogel led to similar gastric protein digestibility. In contrast, in the case of the FLX oleogel, gastric proteolysis decreased to 40%, suggesting a role of the oil nature in steering WP aerogel digestion. In all cases, upon intestinal digestion aerogel proteins resulted completely hydrolysed. The lipolysis degree of SO (75%) and FLX (34%) oil in the oleogels was higher than that of the unstructured SO (66%) and FLX (24%) oils, due to the larger surface offered by smaller oil droplets to the action of intestinal lipases. This was confirmed by dynamic light scattering, showing a shift towards smaller size in the digestive micelle distribution of oleogels at the end of the intestinal phase. Oleogelation through the WP aerogel-template approach could be regarded as a strategy to steer lipid digestibility while also modulating the release of bioaccessible peptides.

In vitro digestion nullified the differences triggered by roasting in phenolic composition and α-glucosidase inhibitory capacity of coffee.

Coffee beans were roasted to medium, dark and very dark degrees, and respective brews were in vitro digested and tested for α-glucosidase inhibition, to explore their antidiabetic potential. Phenolic acids (PA) and Maillard reaction indices (MRI) were quantified before and after digestion. Molecular docking was carried out to investigate α-glucosidase inhibition mechanisms. In vitro digested coffee inhibited α-glucosidase more effectively, compared to undigested samples, but without differences between roasting degrees. The inhibitory effect may be attributed to chlorogenic acids (CGA), which were the most abundant PA in digested coffees. In fact, molecular docking predicted a high affinity of CGA for α-glucosidase. Even though digestion nullified roasting-induced differences in α-glucosidase inhibition, CGA showed a decreasing trend upon digestion. Similarly, MRI did not differ among coffees upon digestion but decreased compared to undigested samples. Overall, the results reported in this study suggest that the presence of different compounds in coffee matrix may contribute to an antidiabetic effect.

Effect of different oleogelators on lipolysis and curcuminoid bioaccessibility upon in vitro digestion of sunflower oil oleogels.

Sunflower oil enriched with curcuminoid compounds (CUs) was gelled by adding 5% (w/w) saturated monoglycerides (MG), rice bran waxes (RW) or a mixture of ß-sitosterol and γ-oryzanol (PS). The resulting oleogels differed for rheological properties and firmness due to the difference in gel network structure. PS oleogel was the firmest sample followed by RW and MG ones. Upon in vitro digestion, fatty acid release as a function of digestion time was greatly affected by oleogel structure: the extent of lipolysis decreased as oleogel strength increased (PS < RW < MG). On the other hand, the nature of the oleogelator affected CUs bioaccessibility, which was lower in oleogels containing crystalline particles (MG and RW). These findings appear interesting in the attempt to develop oleogels able to control lipid digestion as well as to deliver bioactive molecules in food systems.

Effect of coffee roasting on in vitro α-glucosidase activity: Inhibition and mechanism of action.

In vitro α-glucosidase inhibitory activity of unroasted, and medium, dark and very dark roasted robusta coffee was studied. Coffee extracts significantly inhibited the enzyme activity in a dose-dependent way. The inhibitory activity was well correlated with the degree of roast. Coffee components were separated by gel permeation chromatography into low (1 < MW < 6 kDa), intermediate (15 < MW < 60 kDa) and high (MW > 100 kDa) molecular weight fractions, which were analyzed for the α-glucosidase inhibitory capacity. Only fractions obtained from dark and very dark roasted coffee exhibited inhibitory effect. When the same fraction was obtained from coffee presenting different roasting degree, changes in α-glucosidase inhibition extent were observed. This was attributed to compositional changes within each fraction as induced by roasting. Coffee extracts and their fractions exerted a mixed-type to competitive inhibition against α-glucosidase and these mechanisms are consistent with the complexity of coffee composition.