Begum Altintas

Immobilization of laccase onto spacer-arm attached non-porous poly(GMA/EGDMA) beads: Application for textile dye degradation

Non-porous poly(glycidyl methacrylate/ethyleneglycol dimetacrylate) (poly(GMA/EGDMA)) beads were prepared by suspension polymerization. The enzyme (i.e. laccase) was covalently immobilized onto plain and spacer-arm attached poly(GMA/EGDMA) beads. The amount of immobilized enzyme on the plain and spacer-arm attached beads was determined as 5.6 and 4.9 mg/g, respectively. The maximum activity (V(max)) and Michaelis constant (K(m)) of laccase immobilized on the spacer-arm attached beads, were found to be 77.6 U/min and 0.47 mM, respectively. Finally, the immobilized laccase was operated in a batch system, and textile dye Reactive Red 120 was successfully decolorized in the enzyme reactor.

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.

Amine functional monodisperse microbeads via precipitation polymerization of N-vinyl formamide: immobilized laccase for benzidine based dyes degradation.

Densely cross-linked poly(vinylamine) microbeads (∼ 2 μm) were prepared by precipitation copolymerization of N-vinyl formamide and ethylene glycoldimethacrylate in acetonitrile. The formamido groups of the microbeads were hydrolyzed into amino groups. Then, amino-functionalized microbeads were used for covalent immobilization of laccase via glutaraldehyde coupling. The average amount of immobilized enzyme was 18.7 mg/g microbeads. Kinetic parameters, V(max) and K(m) values were determined as 20.7 U/mg protein and 2.76 × 10(-2)mmol/L for free enzyme and 15.8 U/mg protein and 4.65 mmol/L for the immobilized laccase, respectively. The immobilized laccase was operated in a batch reactor for the degradation of two different benzidine based dyes (i.e., Direct Blue 1 and Direct Red 128). The laccase immobilized on the microbeads was very effective for removal of these dyes which interfere with the hormonal system.

Reversible immobilization of glucose oxidase on polyaniline grafted polyacrylonitrile conductive composite membrane.

Polyacrylonitrile membrane surfaces were modified with chemical polymerization of conductive polyaniline. The effect of aniline concentration on the grafting efficiency was investigated. As the amount of grafted PANI increased on the PAN membrane, the electrical resistance of composite membrane decreased. Composite (PAN/PANI)-1-5 membrane were used for reversible immobilization of GOD. The immobilization efficiency and the activity of the immobilized GOD were increased with increasing PANI contents of the composite membrane. The maximum amount of immobilized enzyme into composite PAN/PANI-5 membrane containing 2.1% PANI was about 251 microg/cm(2). Immobilized GOD exhibited 66% of its original activity even after two months of storage at 4 degrees C while the free enzyme lost its initial activity after three weeks.