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Laccase Immobilization Onto Magnetic Β-Cyclodextrin-Modified Chitosan: Improved Enzyme Stability and Efficient Performance for Phenolic Compounds Elimination Publisher



Tarasi R1 ; Alipour M2 ; Gorgannezhad L3 ; Imanparast S4 ; Yousefiahmadipour A4 ; Ramezani A1 ; Ganjali MR5, 6 ; Shafiee A2 ; Faramarzi MA4 ; Khoobi M2, 7
Authors
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Authors Affiliations
  1. 1. Department of Chemistry, University of Zanjan, Zanjan, Iran
  2. 2. The Institute of Pharmaceutical Sciences, Tehran University of Medical Sciences, Tehran, 1417614411, Iran
  3. 3. School of Natural Sciences, Griffith University, Nathan Campus, Nathan, 4111, QLD, Australia
  4. 4. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, P.O. Box 14155–6451, Tehran, 1417614411, Iran
  5. 5. Center of Excellence in Electrochemistry, Faculty of Chemistry, University of Tehran, Tehran, Iran
  6. 6. Biosensor Research Center, Endocrinology & Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran
  7. 7. Department of Pharmaceutical Biomaterials and Medical Biomaterials Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155–6451, Tehran, 1417614411, Iran

Source: Macromolecular Research Published:2018


Abstract

Three types of improved Fe3O4 magnetic nanoparticles (MNPs), including poly(amidoisophthalicacid) coated magnetite nanoparticles (Fe@PA), cyclodextrin (CD) anchored Fe@PA (Fe@PA-CD), and chitosan (Cs) coated Fe@PA-CD (Fe@PACD-Cs) were successfully developed and characterized. Laccase immobilization onto MNPs was carried out via physical adsorption. The maximal and minimal loading capacity were obtained for Fe@PA and Fe@PA-CD-Cs, respectively. Fe@PA-CDCs-laccase exhibited around 100% of the maximum activity at pH 4 and maintained 70% of its initial activity within the temperature range of 15–55 °C; and Cs coated nanoparticles were more efficient than non-coated. Fe@PA-CD-Cs-laccase maintained 70% of its initial activity up to 12 d from the first day of storage at 25 °C whereas the free laccase, Fe@PA-laccase, and Fe@PA-CD-laccase kept 10%, 28%, and 33% of initial activity, respectively. Furthermore, bio-removal of phenolic compounds was performed by the free and immobilized enzyme. Fe@PA-CD-Cs-laccase showed maximal removal with 96.4% and 85.5% for phenol and bisphenol A, respectively. It seems that Fe@PA-CD-Cs could be an appropriate support for immobilization of other enzymes in various industrial application especially bioremoval of phenolic compounds. [Figure not available: see fulltext.]. © 2018, The Polymer Society of Korea and Springer Science+Business Media B.V., part of Springer Nature.