Immobilization of laccase on itaconic acid grafted and Cu(II) ion chelated chitosan membrane for bioremediation of hazardous materials
Journal of Chemical Technology and Biotechnology
MetadataShow full item record
Please cite this item using this persistent URLhttp://hdl.handle.net/11693/21518
Background: Chitosan membranes were formed through a phase inversion technique and then cross-linked with epichlorohydrin (CHX). Heterogeneous graft copolymerization of itaconic acid (IA) onto membrane was carried out with different monomer concentrations (CHX-g-p(IA)). The membrane properties such as equilibrium swelling ratio, porosity, and contact angle were measured, together with analysis by scanning electron microscopy (SEM), energy dispersive analysis of X-rays (EDAX), atomic force microscopy (AFM), and Fourier transform infrared (FTIR) spectroscopy. Results: The Cu(II) ion incorporated membranes (i.e. CHX-g-p(IA)-Cu(II)) were used for reversible immobilization of laccase using CHX-g-p(IA) membrane as a control system. Maximum laccase adsorption capacities of the CHX-g-p(IA) and CHX-g-p(IA)-Cu(II) membranes (with 9.7% grafting yield) were found to be 6.3 and 17.6 mg mL -1 membrane at pH 4.0 and 6.0, respectively. The K m value for immobilized laccase on CHX-g-p(IA)-Cu(II) (4.16 × 10 -2 mmol L -1) was 2.11-fold higher than that of free enzyme (1.97 × 10 -2 mmol L -1). Finally, the immobilized laccase was used in a batch system for degradation of three different dyes (Reactive Black 5, RB5; Cibacron Blue F3GA, CB; and Methyl Orange, MO). The immobilized laccase on CHX-g-p(IA)-Cu(II) membrane was more effective for removal of MO dye than removal of CB and RB5 dyes. CONCLUSION: Flexibility of the enzyme immobilized grafted polymer chains is expected to provide easy reaction conditions without diffusion limitation for substrate dye molecules and their products. The support described, prepared from green chemicals, can be used for the immobilization of industrially important enzymes. © 2012 Society of Chemical Industry.
- Research Paper 7144
Showing items related by title, author, creator and subject.
Selampinar F.; Akbulut, U.; Özden, M.Y.; Toppare L. (Elsevier Science Ltd, Oxford, United Kingdom, 1997)This paper reports a novel approach in the electrode immobilization of an enzyme, invertase, by electrochemical polymerization of pyrrole in the presence of enzyme. The polypyrrole/invertase and polyamide/polypyrrole/invertase ...
Bioactive surface design based on functional composite electrospun nanofibers for biomolecule immobilization and biosensor applications Demirci Uzun, S.; Kayaci F.; Uyar, T.; Timur, S.; Toppare L. (American Chemical Society, 2014)The combination of nanomaterials and conducting polymers attracted remarkable attention for development of new immobilization matrices for enzymes. Hereby, an efficient surface design was investigated by modifying the ...
Inanç, E.; Miller J.E.; DiBiasio, D. (John Wiley & Sons Inc, New York, NY, United States, 1996)The effect of reduced oxygen supply on the production of a recombinant protein (plasmid-encoded β-galactosidase) was investigated in Escherichia coli. A novel modified bubble tank reactor was used to provide a direct ...