Identification and characterization of a novel thermo-stable endo-β-N-acetylglucosaminidase from Rhizomucorpusillus.

Endo-β-N-acetylglucosaminidase (ENGase) is an enzyme that hydrolyzes the chitobiose core of N-glycans and is widely used for glycan analysis on glycoproteins and preparation of precursors for glycosylated compounds. While most of the ENGases that can hydrolyze complex-type glycans are derived from eukaryotes, their production by heterologous expression using Escherichia coli is insufficient, making the production process expensive. From an industrial perspective, there is a need for a less expensive enzyme with higher activity and stability.

Syntheses and antimicrobial activities of ogipeptin derivatives.

Novel cyclic peptide derivatives based on ogipeptins A, B, C, and D were synthesized. Starting with a mixture of ogipeptins A-D, a practical four-step synthetic procedure was followed to prepare novel derivatives with various kinds of acyl side chains. Among the 45 new synthetic derivatives identified, the antibacterial activities of compounds 8-3 and 8-38 were comparable with those of ogipeptin A.

Biosynthesis of nectrisine in Thelonectria discophora SANK 18292.

Nectrisine, an iminosugar with a heterocyclic nitrogen-containing 5-membered ring, acts as a glycosidase inhibitor. Thelonectria discophora SANK 18292, a fungus, was identified as a nectrisine producer from its microbial library in our screening for nectrisine producing microorganisms. Biosynthesis of nectrisine produced by the fungus was studied using stable isotope tracer techniques.

Property development for biaxial drawing of ethylene-tetrafluoroehtylene copolymer films and resultant fractural behavior analyzed by in situ X-ray measurements.

The property development of the ethylene-tetrafluoroethylene copolymer (ETFE) membrane induced by simultaneous biaxial drawing was investigated. Commonly, tensile strength can be increased by drawing; conversely, tear resistance decreases. In this study, the balance between tensile strength and tear resistance for the resultant ETFE membrane was optimized achieved by a combination of lamination of low molecular weight (LMW) and high molecular weight (HMW) layers and subsequent biaxial drawing.

Novel Nrf2 activators from microbial transformation products inhibit blood-retinal barrier permeability in rabbits.

Background And Purpose: Nuclear factor erythroid 2-related factor 2 (Nrf2) is a redox-sensitive transcription factor that binds to antioxidant response elements located in the promoter region of genes encoding many antioxidant enzymes and phase II detoxifying enzymes. Activation of the Nrf2 pathway seems protective for many organs, and although a well-known Nrf2 activator, bardoxolone methyl, was evaluated clinically for treating chronic kidney disease, it was found to induce adverse events. Many bardoxolone methyl derivatives, mostly derived by chemical modifications, have already been studied.

Haplofungins, novel inositol phosphorylceramide synthase inhibitors, from Lauriomyces bellulus SANK 26899 I. Taxonomy, fermentation, isolation and biological activities.

In the course of screening for antifungal agents, we have discovered eight novel compounds, haplofungin A, B, C, D, E, F, G and H, from a culture broth of the fungus strain Lauriomyces bellulus SANK 26899. Haplofungins are composed of an arabinonic acid moiety linked through an ester to a modified long alkyl chain and show potent inhibitory activities against fungal inositol phosphorylceramide (IPC) synthase. Haplofungin A inhibited the activity of IPC synthase from Saccharomyces cerevisiae with an IC(50) value of 0.

Ascotricins A and B, novel antagonists of sphingosine-1-phosphate receptor 1 from Ascotricha chartarum Berk. SANK 14186.

Ascotricins A and B were isolated as novel sphingosine-1-phosphate receptor 1 (S1P(1)) antagonists from a cultured broth of a fungus identified as Ascotricha chartarum Berk. SANK 14186. The two compounds were purified by solvent extraction, reversed-phase (RP) column chromatography and a preparative RP-HPLC.

Colletoic acid, a novel 11beta-hydroxysteroid dehydrogenase type 1 inhibitor from Colletotrichum gloeosporioides SANK 21404.

Colletoic acid, a novel 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) inhibitor, was found and isolated from the cultured broth of the producing fungus Colletotrichum gloeosporioides SANK 21404. Its structure was determined to be a novel acorene-type sesquiterpene by several spectroscopic methods. The absolute structure of colletoic acid was established using a modified Mosher's method and single-crystal X-ray diffraction analysis.