Bipolar Membranes for Direct Borohydride Fuel Cells-A Review.

Direct liquid fuel cells (DLFCs) operate directly on liquid fuel instead of hydrogen, as in proton-exchange membrane fuel cells. DLFCs have the advantages of higher energy densities and fewer issues with the transportation and storage of their fuels compared with compressed hydrogen and are adapted to mobile applications. Among DLFCs, the direct borohydride-hydrogen peroxide fuel cell (DBPFC) is one of the most promising liquid fuel cell technologies.

Two-in-One Surfactant Disinfectant Potential of Xylitol Dicaprylate and Dilaurate Esters Synthesized by Talaromyces thermophilus galactolipase for Cleaning Industries.

Talaromyces thermophilus galactolipase (TTL) was found to produce alcohol sugar fatty acid diesters. The modulation of the solvent composition was used for the esterification reaction screening of diesters from xylitol and various fatty acids using the immobilized Talaromyces thermophilus galactolipase. The reactions were assessed by LC-MS analysis.

Galactolipase activity of Talaromyces thermophilus lipase on galactolipid micelles, monomolecular films and UV-absorbing surface-coated substrate.

Talaromyces thermophilus lipase (TTL) was found to hydrolyze monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates presented in various forms to the enzyme. Different assay techniques were used for each substrate: pHstat with dioctanoyl galactolipid-bile salt mixed micelles, barostat with dilauroyl galactolipid monomolecular films spread at the air-water interface, and UV absorption using a novel MGDG substrate containing α-eleostearic acid as chromophore and coated on microtiter plates. The kinetic properties of TTL were compared to those of the homologous lipase from Thermomyces lanuginosus (TLL), guinea pig pancreatic lipase-related protein 2 and Fusarium solani cutinase.

Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization.

A thermostable xylanase from a newly isolated thermophilic fungus Talaromyces thermophilus was purified and characterized. The enzyme was purified to homogeneity by ammonium sulfate precipitation, diethylaminoethyl cellulose anion exchange chromatography, P-100 gel filtration, and Mono Q chromatography with a 23-fold increase in specific activity and 17.5% recovery.