In-vitro cytotoxic activities of poly(2-ethyl-2-oxazoline)-based amphiphilic block copolymers prepared by CuAAC click chemistry

Synthesis and characterization of well-defined amphiphilic block copolymers containing poly(2-ethyl-2-oxazoline) as hydrophilic block and poly(ε-caprolactone) or poly(L-lactide) as hydrophobic block is achieved by copper-catalyzed azide-alkyne cycloaddition (CuAAC) click chemistry. The clickable precursors, α-alkyne-functionalized poly(ε-caprolactone) and poly(L-lactide) and ω-azido-functionalized poly(2-ethyl-2-oxazoline) are simply prepared and joined using copper sulfate/ascorbic acid catalyst system at room temperature. The structures of precursors and amphiphilic block copolymers are characterized by spectroscopic, chromatographic and thermal analyses. The cytotoxic activities of resulting amphiphilic block copolymers and their precursors are investigated in the prostate epithelial and cancer cells under in-vitro conditions. The treatment of the healthy prostate epithelial cell line PNT1A reveals that no significant cytotoxicity, whereas some significant toxic effects on the prostate cancer cell lines are observed

Polysaccharidase and glycosidase production of avicel grown rumen fungus Orpinomyces sp. GMLF5

Extracellular and cell-associated enzyme preparations were obtained from ruminal anaerobic fungi Orpinomyces sp. GMLF5 grown in culture containing microcrystalline cellulose (avicel) as sole energy source and degradation capacities of the preparations towards several polysaccharides and glycosides were studied. Fungus showed substantial increases in xylanase, carboxymethyl cellulase (CMCase), lichenase, amylase, β-xylosidase, β-glucosidase and α-L-arabinofuranosidase activities between 72 and 168 hours. High amounts of cell associated β-xylosidase were noted in 4 and 5 days old cultures. Optimum temperature and pH of the polysaccharidases were found at 50 °C and 6.0–6.5, respectively. Xylanase was found to be virtually stable at 50°C, CMCase and lichenase were stable at 40 °C for 200 min, however amylase was found more sensitive to heat treatment. The fibrolytic enzymes of the isolate GMLF5 were observed to be capable of hydrolyze the avicel