Dithiocarbamate to modify magnetic graphene oxide nanocomposite (Fe3O4-GO): A new strategy for covalent enzyme (lipase) immobilization to fabrication a new nanobiocatalyst for enzymatic hydrolysis of PNPD

Mohammad Heidarizadeh; Esmail Doustkhah; Sadegh Rostamnia; Parisa Fathi Rezaei; Farshad Darvishi Harzevili; Behzad Zeynizadeh

doi:10.1016/j.ijbiomac.2017.03.152

Dithiocarbamate to modify magnetic graphene oxide nanocomposite (Fe₃O₄-GO): A new strategy for covalent enzyme (lipase) immobilization to fabrication a new nanobiocatalyst for enzymatic hydrolysis of PNPD

Int J Biol Macromol. 2017 Aug:101:696-702. doi: 10.1016/j.ijbiomac.2017.03.152. Epub 2017 Mar 29.

Authors

Mohammad Heidarizadeh¹, Esmail Doustkhah², Sadegh Rostamnia³, Parisa Fathi Rezaei⁴, Farshad Darvishi Harzevili⁴, Behzad Zeynizadeh⁵

Affiliations

¹ Organic and Nano Group (ONG), Department of Chemistry, Faculty of Science, University of Maragheh, PO Box 55181-83111, Maragheh, Iran; Department of Microbiology, Faculty of Science, University of Maragheh, PO Box 55181-83111, Maragheh, Iran.
² Organic and Nano Group (ONG), Department of Chemistry, Faculty of Science, University of Maragheh, PO Box 55181-83111, Maragheh, Iran; Department of Chemistry, Faculty of Science, Urmia University, Urmia 57159-165, Iran. Electronic address: esmaildostkhah@gmail.com.
³ Organic and Nano Group (ONG), Department of Chemistry, Faculty of Science, University of Maragheh, PO Box 55181-83111, Maragheh, Iran. Electronic address: rostamnia@maragheh.ac.ir.
⁴ Department of Microbiology, Faculty of Science, University of Maragheh, PO Box 55181-83111, Maragheh, Iran.
⁵ Department of Chemistry, Faculty of Science, Urmia University, Urmia 57159-165, Iran. Electronic address: bzeynizadeh@gmail.com.

PMID: 28363653
DOI: 10.1016/j.ijbiomac.2017.03.152

Abstract

Immobilization of lipase was successfully achieved on the surface of magnetically separable Fe₃O₄/graphene oxide (GO) via a post-modification. This post modification was achieved in alternation to glutaraldehyde post-modification. The activity of immobilized lipase had not a significant loss in the activity while on the other hand, it is simply extractable (by keeping its major activity) from reaction crude by a magnet. Each step of immobilization was carefully monitored by characterization and all were successfully proved. SEM, TEM, XRD, EDX, and FTIR were used to characterize the support and immobilization process.

Keywords: Dithiocarbamate; Enzyme immobilization; Graphene oxide; Lipase; Nanocomposite.

MeSH terms

Animals
Biocatalysis*
Enzymes, Immobilized / chemistry
Enzymes, Immobilized / metabolism
Graphite / chemistry*
Hydrolysis
Laurates / metabolism*
Lipase / chemistry*
Lipase / metabolism*
Magnetite Nanoparticles / chemistry*
Models, Molecular
Nanocomposites / chemistry
Nitrobenzenes / metabolism*
Oxides / chemistry
Protein Conformation
Swine
Thiocarbamates / chemistry*

Substances

4-nitrophenyl dodecanoate
Enzymes, Immobilized
Laurates
Magnetite Nanoparticles
Nitrobenzenes
Oxides
Thiocarbamates
Graphite
Lipase