Meltem Yilmaz

Reversible immobilization of laccase to poly(4-vinylpyridine) grafted and Cu(ii) chelated magnetic beads: biodegradation of reactive dyes.

Poly(4-vinyl pyridine), poly(VP), as a novel metal-chelating fibrous polymer was grafted on the magnetic beads. Poly(4-VP) grafted and/or Cu(II) ions chelated magnetic beads were used for reversible immobilization of Trametes versicolor laccase, and the amounts of immobilized laccase on the beads were determined as 36.8 and 56.4 mg/g beads, respectively. The adsorption of laccase on both modified magnetic beads appeared to follow the Langmuir isotherm model. The degradation of textile dyes with immobilized laccase on the metal chelated magnetic beads was evaluated in a batch system. Three different reactive textile dyes (i.e., Reactive Green 19, Reactive Red 2 and Reactive Brown 10) were successfully degraded in the enzyme reactor. It was observed that the decolorization rate varied widely with chemical structure and types of the substitute group of the reactive dye molecules.

Immobilization of catalase via adsorption on poly(styrene-d-glycidylmethacrylate) grafted and tetraethyldiethylenetriamine ligand attached microbeads

Fibrous poly(styrene-d-glycidylmethacrylate) (P(S-GMA)) brushes were grafted on poly(styrene-divinylbenzene) (P(S-DVB)) beads using surface initiated-atom transfer radical polymerization (SI-ATRP). Tetraethyldiethylenetriamine (TEDETA) ligand was incorporated on P(GMA) block. The multi-modal ligand attached beads were used for reversible immobilization of catalase. The influences of pH, ionic strength and initial catalase concentration on the immobilization capacities of the P(S-DVB)-g-P(S-GMA)-TEDETA beads have been investigated. Catalase adsorption capacity of P(S-DVB-g-P(S-GMA)-TEDETA beads was found to be 40.8 ± 1.7 mg/g beads at pH 6.5 (with an initial catalase concentration 1.0mg/mL). The K(m) value for immobilized catalase on the P(S-DVB-g-P(S-GMA)-TEDETA beads (0.43 ± 0.02 mM) was found about 1.7-fold higher than that of free enzyme (0.25 ± 0.03 mM). Optimum operational temperature and pH was increased upon immobilization. The same support was repeatedly used five times for immobilization of catalase after regeneration without significant loss in adsorption capacity or enzyme activity.

Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: Catalytic properties and stabilities

Chloroperoxidase (CPO) was covalently immobilized on poly(hydroxypropyl methacrylate-co-polyethyleneglycole-methacrylate) membranes, which were characterized, by swelling test, FT-IR spectroscopy, scanning electron microscopy, and contact angle measurement. The Km and Vmax values for free and immobilized CPO were found to be 34.6 and 47.2 μM, and 287.5 and 245.2 U/mg protein, respectively. The optimum pH for both the free and immobilized enzyme was observed at 3.0. The immobilized enzyme showed wide pH and temperature profiles. Most importantly, the increased thermal, storage and operational stability of immobilized CPO should depend on the creation of a comfortable strong hydrophilic microenvironment on the designed support to the host enzyme molecule.

Immobilization and stabilization of papain on poly(hydroxyethyl methacrylate-ethylenglycol dimethacrylate) beads grafted with epoxy functional polymer chains via surface-initiated-atom transfer radical polymerization (SI-ATRP).

Poly(hydroxyethyl methacrylate-ethylen glycol dimethacrylate), p(HEMA-EGDMA), beads were prepared by suspension polymerization, and were decorated with fibrous poly(glycidyl methacrylate), p(GMA), via surface initiated-atom transfer radical polymerization (SI-ATRP). The functional epoxy groups of the beads were used for covalent immobilization of papain. The average amount of immobilized enzyme was 18.7 mg/g beads. The immobilized enzyme was characterized by temperature, pH, operational and storage stability experiments. The maximum velocity of the free and immobilized enzymes (V(max)) and Michaelis-Menten constant (K(m)) values were determined as 10.7 and 8.3 U/mg proteins and 274 and 465 μM, respectively. The immobilized papain was operated in a batch reactor, and it was very effective for hydrolysis of different proteins (i.e., casein and cytochrom c).

Azo Dye Removal Using Free and Immobilized Fungal Biomasses: Isotherms, Kinetics and Thermodynamic Studies

In this study, Lentinus concinnus biomass was immobilized in polyvinyl alcohol/polyethyleneoxide hydrogels (PVA/PEO; referred as composite biomass) and used for removal of Reactive Yellow 86 dye (RY-86) from aqueous solution using free fungal biomass as a control system. The free fungal and composite fungal biomasses were characterized using ATR-FTIR, SEM and analytical methods. FTIR studies of the adsorbent preparations show that carboxylate, hydroxyl and amine groups should be involved in adsorption of the RY-86 dye. The adsorption of RY-86 dye on these adsorbents increased as the initial concentration of RY-86 dye in the medium increased up to 200 mg/l. The maximum RY-86 dye adsorption for the free fungal and composite fungal biomasses, was obtained as 190.2 and 87.6, respectively, using 200 mg/l initial dye concentration, at 25 °C, and at pH 5.0 with 2.0 h contact. The equilibrium data were well described with the Freundlich and Temkin isotherm models. The adsorption of RY-86 dye was fitted best by the pseudo second-order kinetic model. Thermodynamic parameters (ΔG°, ΔH°, and ΔS°) showed that RY-86 dye adsorption on both adsorbents were spontaneous process.