Fermented oat-based foods offer attractive prospects within the market of non-dairy functional products, since they are suitable substrates for the delivery of probiotic microorganisms, and are significant sources of dietary fiber, both insoluble and soluble such as β-glucan, good quality fat and other phytochemicals important for human health In the present work, whole oat flour was fermented with probiotic Lactobacillus plantarum strains to produce new functional foods with improved nutritional and technological features. Viability of the probiotic and the main technological, physico-chemical, nutritional and sensorial parameters were monitored at 7, 14 and 21 days of cold storage. The microbial survival was higher than 5x10 8 cfu g-1 at the end of the shelf life. After the fermentation step, viscosity was higher in products inoculated with the exopolysaccharide-producing L. plantarum strain Lp90. However, a subsequent viscosity reduction was detected in all the samples throughout the storage period, consistent with the observed concentration decrease of the oat β-glucan. Vitamin B2 content was about twofold higher in products fermented by the riboflavin-overproducing LpB2, and in these samples the riboflavin concentration further increased during cold storage. Highlights  Fermented oat-based foods are suitable substrates for delivery probiotic LAB.  Riboflavin-overproducing LpB2 increased the vitamin B2 content of oat-based products.  EPS-producing Lp90 seems to improve some rheological features.

Here we report the cloning, expression, and characterization of a cAMP-specific phosphodiesterase (PDE) from Trypanosoma brucei (TbPDE2B). Using a bioinformatic approach, two different expressed sequence tag clones were identified and used to isolate the complete sequence of two identical PDE genes arranged in tandem. Each gene consists of 2,793 bases that predict a protein of 930 aa with a molecular mass of 103.2 kDa. Two GAF (for cGMP binding and stimulated PDEs, Anabaena adenylyl cyclases, and Escherichia coli FhlA) domains, similar to those contained in many signaling molecules including mammalian PDE2, PDE5, PDE6, PDE10, and PDE11, were located N-terminal to a consensus PDE catalytic domain. The catalytic domain is homologous to the catalytic domain of all 11 mammalian PDEs, the Dictyostelium discoideum RegA, and a probable PDE from Caenorhabditis elegans. It is most similar to the T. brucei PDE2A (89% identity). TbPDE2B has substrate specificity for cAMP with a K m of 2.4 M. cGMP is not hydrolyzed by TbPDE2B nor does this cyclic nucleotide modulate cAMP PDE activity. The nonselective PDE inhibitors 3-isobutyl-1-methylxanthine, papaverine and pentoxifyline are poor inhibitors of TbPDE2B. Similarly, PDE inhibitors selective for the mammalian PDE families 2, 3, 5, and 6 (erythro-9-[3-(2-hydroxynonyl)]-adenine, enoximone, zaprinast, and sildenafil) were also unable to inhibit this enzyme. However, dipyridamole was a reasonably good inhibitor of this enzyme with an IC50 of 27 M. cAMP plays key roles in cell growth and differentiation in this parasite, and PDEs are responsible for the hydrolysis of this important second messenger. Therefore, parasite PDEs, including this one, have the potential to be attractive targets for selective drug design.inhibitors ͉ GAF domain

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