Performance of microbial phytases for gastric inositol phosphate degradation

Anne Veller Friis Nielsen, Christian Nyffenegger, Anne S. Meyer

Research output: Contribution to journalJournal articlepeer-review


Microbial phytases catalyze dephosphorylation of phytic acid, thereby potentially releasing chelated iron and improving human iron absorption from cereal-based diets. For this catalysis to take place in vivo, the phytase must be robust to low pH and proteolysis in the gastric ventricle. This study compares the robustness of five different microbial phytases, evaluating thermal stability, activity retention, and extent of dephosphorylation of phytic acid in a simulated low-pH/pepsin gastric environment and examines secondary protein structural changes at low pH via circular dichroism. The Peniophora lycii phytase was found to be the most thermostable, but the least robust enzyme in gastric conditions, whereas the Aspergillus niger and Escherichia coli phytases proved to be most resistant to gastric conditions. The phytase from Citrobacter braakii showed intermediate robustness. The extent of loss of secondary structure at low pH correlated positively with the extent of activity loss at low pH.
Original languageEnglish
JournalJournal of Agricultural and Food Chemistry
Issue number3
Pages (from-to)943-950
Publication statusPublished - 2015


  • Circular dichroism
  • Digestion
  • Enzyme
  • Food
  • Gastrointestinal tract
  • In vitro
  • Iron
  • Pepsin
  • pH stability
  • Phytate
  • Phytic acid
  • Proteolysis
  • Secondary structure
  • Thermostability
  • Aspergillus
  • Dichroism
  • Escherichia coli
  • Food products
  • pH effects
  • Sludge digestion
  • In-vitro
  • PH stability
  • Phytic acids
  • Secondary structures
  • Enzymes


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