FUNCTIONAL FOOD BASED ON A COMBINATION OF POLYPHENOLS AND POLYSACCHARIDES WITH EMERGENT PROPERTIES FOR HYPOCALORIC DIET

The aim of this work was to develop a functional food used as an adjuvant for hypocaloric diet, based on a combination of polyphenols and polysaccharides extracted from berries pomace and chia seeds, presenting emergent properties. These bioactive compounds were encapsulated into liposomes before being added in the composition of a new protein bar. The antioxidant activity of polyphenols- polysaccharides combinations in different ratios was determined by TEAC and DPPH assays. It was observed that the mixture of polyphenols extracted from berries and polysaccharides extracted from chia seeds in a weight ratio of 5:1 had the highest antioxidant activity. A study of α-amylase inhibition in the presence of polyphenols, polysaccharides and their combinations was also performed to investigate the synergism of these compounds. A liposomal formulation of the selected synergistic combination was obtained in powder form by lyophilization. A final product including the synergistic combination was prepared in the form of a hypoglycemic food bar with amplified antioxidant effects. The product is further recommended for potential application as an adjuvant for a low-calorie diet

EDEM3 Domains Cooperate to Perform Its Overall Cell Functioning

EDEM3 recognizes and directs misfolded proteins to the ER-associated protein degradation (ERAD) process. EDEM3 was predicted to act as lectin or as a mannosidase because of its homology with the GH47 catalytic domain of the Man1B1, but the contribution of the other regions remained unresolved. Here, we dissect the molecular determinants governing EDEM3 function and its cellular interactions. LC/MS analysis indicates very few stable ER interactors, suggesting EDEM3 availability for transient substrate interactions. Sequence analysis reveals that EDEM3 consists of four consecutive modules defined as GH47, intermediate (IMD), protease-associated (PA), and intrinsically disordered (IDD) domain. Using an EDEM3 knock-out cell line, we expressed EDEM3 and domain deletion mutants to address EDEM3 function. We find that the mannosidase domain provides substrate binding even in the absence of mannose trimming and requires the IMD domain for folding. The PA and IDD domains deletions do not impair the trimming, but specifically modulate the turnover of two misfolded proteins, NHK and the soluble tyrosinase mutant. Hence, we demonstrate that EDEM3 provides a unique ERAD timing to misfolded glycoproteins, not only by its mannose trimming activity, but also by the positive and negative feedback modulated by the protease-associated and intrinsically disordered domain, respectively