Biosorption kinetics of a direct azo dye Sirius Blue K-CFN by Trametes versicolor

In this study, lyophilized Trametes versicolor biomass is used as a sorbent for biosorption of a textile dye, Sirius Blue K-CFN, from an aqueous solution. The batch sorption was studied with respect to dye concentration, adsorbent dose and equilibrium time. The effect of pH and temperature on dye uptake was also investigated and kinetic parameters were determined. Optimal initial pH (3.0), equilibrium time (2 hrs), initial dye concentration ( 100 mg l-1) and biomass concentration (1.2 mg l-1) were determined at 26\ubaC. The maximum biosorption capacity (qmax) of Sirius Blue K-CFN dye on lyophilized T. versicolor biomass is 62.62 mg/g. The kinetic and isotherm studies indicated that the biosorption process obeys to a pseudo-second order model and Langmuir isotherm model. In addition, the biosorption capacities of fungal biomass compared to other well known adsorbents such as activated carbon and Amberlite, fungal biomass biosorptions capacities were found to be more efficient

Biodegradation kinetics of o-cresol by Pseudomonas putida DSM 548 (pJP4) and o-cresol removal in a batch-recirculation bioreactor system

The biodegradation kinetics of o-cresol was examined by acclimatized P. putida DSM 548 (pJP4) in batch experiments at varying initial o-cresol concentrations (from 50 to 500 mg/L). The kinetic parameters of o-cresol aerobic biodegradation were estimated by using the Haldane substrate inhibition equation. The biodegradation kinetics of o-cresol was investigated. In batch culture reactors, the Maximum specific growth rate (\u3bcmax), Monod constant (Ks) and the inhibition constant (Ki) were established as 0.519 h-1, 223.84 mg/L and 130.883 mg/L, respectively. o-cresol biodegradation in a batch-recirculation bioreactor system by immobilized P. putida was also studied. The recycled packed bed reactor system, which was composed of Ca-alginate beads and pumice on which cells immobilized, has been performed to determine possible stability for further developments

THROMBIN IMMOBILIZATION TO METHACRYLIC ACID GRAFTED POLY(3-HYDROXYBUTYRATE) AND ITS IN VITRO APPLICATION

WOS: 000312186100004PubMed ID: 23215654Poly(3-hydroxybutyrate) is nontoxic and biodegradable, with good biocompatibility and potential support for long-term implants. For this reason, it is a good support for enzyme immobilization. Enzyme immobilization could not be done directly because poly(3-hydroxybutyrate) has no functional groups. Therefore, modification should be done for enzyme immobilization. In this study, methacrylic acid was graft polymerized to poly(3-hydroxybutyrate) and thrombin was immobilized to polymethacrylic acid grafted poly(3-hydroxybutyrate). In fact, graft polymerization of methacrylic acid to poly(3-hydroxybutyrate) and thrombin immobilization was a model study. Biomolecule immobilized poly(3-hydroxybutyrate) could be used as an implant. Thrombin was selected as a biomolecule for this model study and it was immobilized to methacrylic acid grafted poly(3-hydroxybutyrate). Then the developed product was used to stop bleeding

Immobilization of Thrombin to Bio/Chemically Modified Synthetic Fabrics

14th National Biomedical Engineering Meeting -- MAY 20-22, 2009 -- Izmir, TURKEYWOS: 000274345400098Processed synthetic polymers used in medical textile are used directly or functionalized by immobilization of bioactive molecules. Textile products made by synthetic polymers are durable, resistant to chemical reactions and have inert structures. Textile products made by synthetic polymers usually have not functional groups for immobilization. So modification could be done for formation of functional groups. Immobilization of bioactive molecules could be done by functional groups. In this study, thrombin was immobilized to textile products made by synthetic polymers. So Textile products made by synthetic polymers was added a now character which was blood stopper. The product was reliable because of source

Thrombin immobilization to enzymatic modified PET and PAN fabrics and their applications

WOS: 000310468000005Enzymatic modification of synthetic materials has immense potential both of the functionalization of polymeric materials, such as poly(acrylonitrile) or polyesters, and the production of polymers for special applications, such as medical devices and enzyme immobilization. In this study, poly(ethyleneterephtalate) and poly(acrylonitrile) fabrics were modified with commercial laccase and nitrilase, respectively. Contact angles of enzymatic modified and unmodified fabrics were measured and it was found contact angles of enzymatic modified fabrics were less than those of unmodified fabrics. Attenuated-Total-Reflection-Fourier-Transform infrared spectroscopy showed that carboxylic acid groups occurred on fabrics after enzymatic modifications. Surfaces of modified and unmodified fabrics were investigated using scanning electron microscopy. Surfaces of unmodified fabrics were smooth but surfaces of modified fabrics were rugged and cracked. Thrombin was immobilized in modified fabrics by using 1-Ethyl-3-(3-dimetylaminopropyl)-carbodiimide. Optimization studies were also performed for the immobilization of thrombin. After prepared material was tested to stop bleeding in vitro conditions and it was found that thrombin immobilized poly(ethyleneterephtalate) and poly(acrylonitrile) fabrics had a reduced recalcification time to 51 % and 89 %, respectively. Thrombin immobilized poly(ethyleneterephtalate) fabric was also tested in in vivo conditions by using Cavia porcellus and it was observed that this material caused bleeding to stop at a ratio of 24.6 %. The results were statistically significant.Ege University Research FoundationEge University [2007 FEN 010]This work was supported by Ege University Research Foundation 2007 FEN 010

Thrombin immobilization to Poly(Methacrylicacid) graft polymerized PET and PAN fabrics

WOS: 000317352500003Poly(ethylene terephthalate) and poly(acrylonitrile) fabrics are the most produced synthetic fabrics in the world. Their production and usage increase at medical textile. There is no functional group in their structure for enzyme immobilization. Hence, they are not inclined to react. However, functional groups could be added to their structure using graft polymerization. In this study, methacrylic acid was graft polymerized to poly(ethylene terephthalate) and poly(acylonitrile) fabrics. Characterization of modified fabrics was carried out and thrombin was immobilized to poly(methacrylic acid) graft polymerized poly(ethylene terephthalate) and poly(acylonitrile) fabrics using 1-Ethyl-3-(3-dimetylaminopropyl)-carbodiimide. Optimization studies were also performed for the immobilization of thrombin. Thrombin immobilized poly(methacrylic acid) graft polymerized poly(ethylene terephtalate) and poly(acrylonitrile) fabrics were reduced recalcification time 30 % and 25 %, respectively. It is the first time, an enzyme was immobilized to fabric and its in vitro applications were performed. Thrombin has not been immobilized to synthetic fabric, yet.Ege University Research FoundationEge University [2007FEN010]This work was supported by Ege University Research Foundation 2007FEN010

Enhanced production of manganese peroxidase by Phanerochaete chrysosporium

WOS: 000254142000001Production of manganese-dependent peroxidase (MnP) by the white-rot fungus Phanerochaete chrysosporium BKM-F-1767 (ATCC 24725) was monitored during growth in different media and growth conditions. The effect of some activators of MnP production, Mn2+, Tween 80, phenylmethylsulphonylfloride (PMSF), oxygen, temperature, pH, glycerol and nitrogen was studied. Supplementing the cultures with Tween 80 (0.05 %, v/v) and Mn2+ (174 mu M) resulted a maximum MnP activity of 356 U/L which was approximately two times higher than that obtained in the control culture (without Tween 80). Decolourisation of Direct Blue 15 and Direct Green 6 (50 mg/L) was also achieved with MnP

Manganese peroxidase production by immobilized Phanerochaete chrysosporium BKM-F-1767 in a cell Bioreactor

WOS: 000252312100001PubMed ID: 18080906Manganese-dependent peroxidase (MnP) production was performed in an immobilized cell bioreactor in which Phanerochaete chrysosporium BKM-F-1767 was immobilized on polystyrene foam. The immobilized cell culture yielded significantly greater MnP activity than the conventional stationary liquid culture. Cultivation was carried out in batch mode; the effect of glucose concentration was investigated and growth kinetics parameters were found as, Am., = 0.59 day(-1), K-S = 0.33 g/L and K-ss = 14.5. Batch operation led to maximum MnP (770.82 U/L) in the culture medium containing 0.05% Tween 80, 10 g/L glucose, and 174 mu M Mn2+ at 37 degrees C and pH 4.5. Enzyme productivity was obtained as 110.12 U/day/L

Production and Gelatin Entrapment of Laccase from Trametes versicolor and its Application to Quantitative Determination of Phenolic Contents of Commercial Fruit Juices

WOS: 000297496100005Laccase (benzenediol: oxygen oxidoreductase; EC 1.10.3.2) is a particularly promising enzyme for several industrial fields, including food industries, since this enzyme catalyzes the oxidation of ortho and para-diphenols, amino-phenols, polyphenols, polyamines, lignins, and aryl diamines as well as some inorganic ions coupled to the reduction of molecular dioxygen to water. In this study, laccase was produced from one of the best laccase-producing organisms, Trametes versicolor. For this purpose, several phenolic acids were tested as laccase inducers. Caffeic acid and ferulic acid were determined to be the best inducers among the tested phenolic acids. Also, it was shown that laccase activity could be determined by using caffeic acid and ferulic acid as phenolic substrates by measuring the rates of oxygen consumption. Laccase was immobilized in gelatin under optimized conditions. Kinetic constants K(m) and V(max) for immobilized enzyme were estimated to be 74.758 mu M and 0.744 mu mol. Delta O(2)/ml. min for caffeic acid and 0.999 mu M and 57.80 mu mol. Delta O(2)/ml. min for ferulic acid, respectively. The immobilized enzyme exhibited the maximal activity at pH 4.5, and at 35 degrees C. Immobilized enzymes were used for the determination phenolic contents of commercially prepared fruit juices. Caffeic acid contents of black cherry, apricot, and peach juice were determined to be 1640 +/- 33, 679 +/- 24 and 408 +/- 29 mg/L, and their ferulic acid contents were determined to be 1786 +/- 28, 800 +/- 30, and 444 +/- 28 mg/L, respectively.Ege UniversityEge University [2004 Fen 07]This work was partly supported by Ege University Scientific Research Fund (2004 Fen 07)