Covalent Immobilization of Penicillin G Acylase onto Fe3O4@Chitosan Magnetic Nanoparticles

J Microbiol Biotechnol. 2016 May 28;26(5):829-36. doi: 10.4014/jmb.1511.11052.

Abstract

Penicillin G acylase (PGA) was immobilized on magnetic Fe3O4@chitosan nanoparticles through the Schiff base reaction. The immobilization conditions were optimized as follows: enzyme/support 8.8 mg/g, pH 6.0, time 40 min, and temperature 25°C. Under these conditions, a high immobilization efficiency of 75% and a protein loading of 6.2 mg/g-support were obtained. Broader working pH and higher thermostability were achieved by the immobilization. In addition, the immobilized PGA retained 75% initial activity after ten cycles. Kinetic parameters Vmax and Km of the free and immobilized PGAs were determined as 0.91 mmol/min and 0.53 mmol/min, and 0.68 mM and 1.19 mM, respectively. Synthesis of amoxicillin with the immobilized PGA was carried out in 40% ethylene glycol at 25°C and a conversion of 72% was obtained. These results showed that the immobilization of PGA onto magnetic chitosan nanoparticles is an efficient and simple way for preparation of stable PGA.

Keywords: Amoxicillin; Chitosan; Immobilization; Magnetic nanoparticles; penicillin G acylase.

MeSH terms

  • Amoxicillin / chemical synthesis
  • Chitosan / chemistry*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / metabolism
  • Ethylene Glycol / chemistry
  • Ferric Compounds / chemistry
  • Magnetite Nanoparticles / chemistry*
  • Microscopy, Electron, Transmission
  • Nanoparticles / chemistry
  • Penicillin Amidase / chemistry*
  • Penicillin Amidase / metabolism

Substances

  • Enzymes, Immobilized
  • Ferric Compounds
  • Magnetite Nanoparticles
  • ferric oxide
  • Amoxicillin
  • Chitosan
  • Penicillin Amidase
  • Ethylene Glycol