Production, purification and properties of microbial phytases

Ashok Pandey, George Szakacs, Carlos R. Soccol, Jose A. Rodriguez-Leon, Vanete T. Soccol

Research output: Contribution to journalArticle

225 Citations (Scopus)


Phytases (myo-inositol hexakisphosphate phosphohydrolase, EC catalyse the release of phosphate from phytate (myco-inositol hexakiphosphate). Several cereal grains, legumes and oilseeds, etc., store phosphorus as phytate. Environmental pollution due to the high-phosphate manure, resulting in the accumulation of P at various locations has raised serious concerns. Phytases appear of significant value in effectively controlling P pollution. They can be produced from a host of sources including plants, animals and micro-organisms. Microbial sources, however, are promising for their commercial exploitations. Strains of Aspergillus sp., chiefly A. ficuum and A. niger have most commonly been employed for industrial purposes. Phytases are considered as a monomeric protein, generally possessing a molecular weight between 40 and 100 kDa. They show broad substrate specificity and have generally pH and temperature optima around 4.5-6.0 and 45-60°C. The crystal structure of phytase has been determined at 2.5 Å resolution. Immobilization of phytase has been found to enhance its thermostability. This article reviews recent trends on the production, purification and properties of microbial phytases.

Original languageEnglish
Pages (from-to)203-214
Number of pages12
JournalBioresource Technology
Issue number3
Publication statusPublished - Jan 1 2001


  • Gene expression
  • Micro-organisms
  • Phytase
  • Properties
  • Purification
  • Solid state fermentation
  • Submerged fermentation

ASJC Scopus subject areas

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

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  • Cite this

    Pandey, A., Szakacs, G., Soccol, C. R., Rodriguez-Leon, J. A., & Soccol, V. T. (2001). Production, purification and properties of microbial phytases. Bioresource Technology, 77(3), 203-214.