The biodegradation of waters polluted by some bisphenols, endowed with endocrine activity, has been studied by means of laccase or tyrosinase immobilized on polyacrylonitrile (PAN) beads. Bisphenol A (BPA), Bisphenol B (BPB), Bisphenol F (BPF) and Tetrachlorobisphenol A (TCBPA) have been used. The laccase-PAN beads system has been characterized as a function of pH, temperature and substrate concentration.
View Article and Find Full Text PDFThe catalytic behavior of a mixture of pectic enzymes, covalently immobilized on different supports (glass microspheres, nylon 6/6 pellets, and PAN beads), was analyzed with a pectin aqueous solution that simulates apple juice. The following parameters were investigated: the rate constant at which pectin hydrolysis is conducted, the time (tau(50)) in which the reduction of 50% of the initial viscosity is reached, and the time (tau(comp,dep)) required to obtain complete depectinization. The best catalytic system was proven to be PAN beads, and their pH and temperature behavior were determined.
View Article and Find Full Text PDFChanges in steady-state UV fluorescence emission from free or immobilizedglucose oxidase have been investigated as a function of glucose concentration.Immobilized GOD has been obtained by entrapment into a gelatine membrane. Changes insteady-state UV fluorescence have been quantitatively characterized by means ofoptokinetic parameters and their values have been compared with those previouslyobtained for FAD fluorescence in the visible range.
View Article and Find Full Text PDFLaccase from Trametes versicolor was immobilized by diazotization on a nylon membrane grafted with glycidil methacrylate, using phenylenediamine as spacer and coupling agent. The behavior of these enzyme derivatives was studied under isothermal and nonisothermal conditions by using syringic acid as substrate, in view of the employment of these membranes in processes of detoxification of vegetation waters from olive oil mills. The pH and temperature dependence of catalytic activity under isothermal conditions has shown that these membranes can be usefully employed under extreme pH and temperatures.
View Article and Find Full Text PDFThe inhibitory power of three different active Nylon membranes, separately loaded with three different protease inhibitors, was studied with the aim of reducing the increased elastase concentration occurring during hemodialysis or extracorporeal blood circulation in patients undergoing cardiopulmonary bypass. Chemical grafting was carried out to make the inert Nylon membrane suitable for the immobilization of the inhibitors. The behavior of immobilized alpha(1)-antitrypsin, bovine pancreatic trypsin inhibitor (BPTI), or elastatinal was separately studied.
View Article and Find Full Text PDFA novel packed-bed bioreactor, operating under isothermal and non-isothermal conditions, has been constructed. The core of the apparatus consisted in a polypropylene ring filled with beta-galactosidase immobilized on beads of polyacrylic acid, grafted with dimethylaminoethyl methacrylate. Phenylendiamine and glutaraldehyde were used as spacer and coupling agent, respectively.
View Article and Find Full Text PDFA hollow-fiber enzyme reactor, operating under isothermal and nonisothermal conditions, was built employing a polypropylene hollow fiber onto which beta-galactosidase was immobilized. Hexamethylenediamine and glutaraldehyde were used as spacer and coupling agent, respectively. Glucose production was studied as a function of temperature, substrate concentration, and size of the transmembrane temperature gradient.
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