Tehran University of Medical Sciences

Science Communicator Platform

Stay connected! Follow us on X network (Twitter):
Share this content! On (X network) By
Lipase Immobilization Onto Polyethylenimine Coated Magnetic Nanoparticles Assisted by Divalent Metal Chelated Ions Publisher



Motevalizadeh SF1, 2 ; Khoobi M1 ; Sadighi A3 ; Khalilvandsedagheh M1 ; Pazhouhandeh M5 ; Ramazani A4 ; Faramarzi MA5 ; Shafiee A1
Authors
Show Affiliations
Authors Affiliations
  1. 1. Department of Medicinal Chemistry, Faculty of Pharmacy and Pharmaceutical Sciences Research Center, Tehran University of Medical Sciences, Tehran, 14176, Iran
  2. 2. Particulate Fluids Processing Centre, School of Chemistry, University of Melbourne, Melbourne, 3010, VIC, Australia
  3. 3. Department of Biomedical and Pharmaceutical Sciences, College of Pharmacy, University of Rhode Island, Kingston, RI, United States
  4. 4. Department of Chemistry, University of Zanjan, P.O. Box 45195-313, Zanjan, Iran
  5. 5. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran, 14176, Iran

Source: Journal of Molecular Catalysis B: Enzymatic Published:2015


Abstract

In this study, polyethylenimine coated Fe3O4 magnetic nanoparticles (Fe@PEI) were prepared and used for three metal ions (Co2+, Cu2+ and Pd2+) chelation. The metal chelated magnetic nanoparticles (Fe@PEI-M) were characterized by using different spectroscopic and analytical techniques. The metal contents were analyzed by inductively coupled plasma atomic emission spectroscopy (ICP) and energy-dispersive X-ray spectroscopy (EDX). Thermomyces lanuginosa lipase (TLL) was then immobilized onto the modified magnetic supports by physical adsorption. Fe@PEI-Co and Fe@PEI-Cu showed better activity at extreme temperature and pH values than of the free enzyme. After 10 cycles of successful biocatalytic activity performed by immobilized lipase on Fe@PEI-Co, more than 60% of initial activity was reserved. Furthermore, the immobilized lipase onto Fe@PEI-Co retained about 80% of its initial activity after 14 days of storage. The immobilized lipase on the selected nanocomposite was then used for synthesis of ethyl valerate. After 24 h incubation time, the extent of esterification was found to be 70 and 60% in n-hexane and DMSO media, respectively. © 2015 Elsevier B.V. All rights reserved.