JR performed most of the experiments involving silencing of GSTT1 and helped with midgut dissections and oocyst counting. GN and GJ-G performed the P. yoelii infections in An. gambiae and An. stephensi. MP and GJ-G silenced TEP1, LRIM1, and LRIM2 in P. yoelii-infected An. gambiae. A M-C prepared the P. falciparum gametocyte cultures. C B-M contributed with experimental design, data analysis, image processing, assembly of final figures, and writing the manuscript.”
“Background Nowadays low-cost

energy bio-industrial processes in biotechnology are Givinostat highly desired. This has led to increased interest in the production of cold adapted enzymes. One class of such enzymes includes cold-adapted β-D-galactosidases (EC 3.2.1.23) that can find many applications in industrial biotechnology. These enzymes are capable of hydrolyzing 1,4-β-D-galactoside linkages and can sometimes catalyse the synthesis of oligosaccharides. The production of lactose-free milk and synthetic oligosaccharides like lactulose are only examples of this cutting edge enzyme class application. Currently, commercially available β-galactosidase preparations (e.g. Lactozym – Novo Nordisk, Maxilact

– DSM Food Specialties) applied for lactose hydrolysis contain Kluyveromyces lactis β-galactosidase naturally intracellularly biosynthesized by K. lactis strains. This enzyme is optimally active at approximately 50°C and displays PFT�� low activity at 20°C while an ideal enzyme Suplatast tosilate for treating milk should work well at 4–8°C. Besides, the latter enzyme should be optimally active at pH 6.7–6.8 and cannot be inhibited

by sodium, calcium or glucose. Such β-galactosidases are still highly desired. Only several enzymes optimally hydrolyzing lactose at low selleck temperatures have been characterized till now [1–14], however, none of them have been produced on the commercial scale. The β-galactosidases were obtained from different microbial sources, including those from Arthrobacter sp. [1, 2, 7, 8, 12], Arthrobacter psychrolactophilus [9, 13]Carnobacterium piscicola [3], Planococcus sp. [4, 14], Pseudoalteromonas haloplanktis [5], and Pseudoalteromonas sp. [10, 11]. Additionally, in order to make progress in cheaper production of β-D-galactosidases of industrial interest, high efficiency yeast expression systems must be taken into consideration. On the other hand extracellular production must occur to allow easy and fast isolation of target protein. There are several studies in literature related to the extracellular production of the Aspergillus niger β-galactosidase by recombinant Saccharomyces cerevisiae strains [15–19], although this enzyme is mainly interesting for lactose hydrolysis in acid whey, because of their acidic pH optimum as well as their activity at elevated temperatures. The S. cerevisiae expression system was also used for the production of K.