Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles

Ralf Greiner*, Ursula Konietzny, Daniel Menezes Blackburn, Milko A. Jorquera

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


Phytases of different origin were covalently bound onto Fe3O4 magnetic nanoparticles (12nm). Binding efficiencies of all three phytases were well above 70% relative to the number of aldehyde groups available on the surface of the magnetic nanoparticles. Temperature stability for all three phytases was enhanced as a consequence of immobilisation, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of the immobilised phytases was found at 60°C (rye), 65°C (Aspergillus niger) and 70°C (Escherichia albertii). The immobilised enzymes exhibited the same excellent substrate specificities and unique myo-inositol phosphate phosphatase activities as their soluble counterparts. However, the catalytic turnover number dropped drastically for the immobilised phytases. The amount of the desired partially phosphorylated myo-inositol phosphate isomer could be easily controlled by the contact time of substrate solution and immobilised enzymes. The immobilised phytases showed a high operational stability by retaining almost full activity even after fifty uses.

Original languageEnglish
Pages (from-to)375-383
Number of pages9
JournalBioresource Technology
Publication statusPublished - Aug 2013


  • Immobilisation
  • Magnetic nanoparticles
  • Myo-inositol phosphates
  • Phytase
  • Phytate

ASJC Scopus subject areas

  • Bioengineering
  • Environmental Engineering
  • Renewable Energy, Sustainability and the Environment
  • Waste Management and Disposal


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