Thermophilic <i>Talaromyces emersonii</i> Flavin Adenine Dinucleotide-Dependent Glucose Dehydrogenase Bioanode for Biosensor and Biofuel Cell Applications

Flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase (GDH) was identified and cloned from thermophilic filamentous fungi Talaromyces emersonii using the homology cloning method. A direct electron transfer bioanode composed of T. emersonii FAD-GDH and a single-walled carbon nanotube was produced. Enzymes from thermophilic microorganisms generally have low activity at ambient temperature; however, the T. emersonii FAD-GDH bioanode exhibits a large anodic current due to the enzymatic reaction (1 mA cm^–2) at ambient temperature. Furthermore, the T. emersonii FAD-GDH bioanode worked at 70 °C for 12 h. This is the first report of a bioanode with a glucose-catalyzing enzyme from a thermophilic microorganism that has potential for biosensor and biofuel cell applications. In addition, we demonstrate how the glycoforms of T. emersonii FAD-GDHs expressed by various hosts influence the electrochemical properties of the bioanode

Crystallization Control and Physicochemical Properties of Polymorphic Forms of the Factor Xa Inhibitor KFA-1982

Many polymorphs of KFA-1982, an orally active factor Xa (fXa) inhibitor, have been identified and their physicochemical properties have been investigated. Form B was selected as the oral API form because of its superior stability and solubility characteristics. Crystallization conditions for form B were thoroughly investigated including the role of water in hydrate formation and the use of antisolvents and supersaturation in polymorph control