New Bacterial Phytase through Metagenomic Prospection

Molecules. 2018 Feb 17;23(2):448. doi: 10.3390/molecules23020448.

Abstract

Alkaline phytases from uncultured microorganisms, which hydrolyze phytate to less phosphorylated myo-inositols and inorganic phosphate, have great potential as additives in agricultural industry. The development of metagenomics has stemmed from the ineluctable evidence that as-yet-uncultured microorganisms represent the vast majority of organisms in most environments on earth. In this study, a gene encoding a phytase was cloned from red rice crop residues and castor bean cake using a metagenomics strategy. The amino acid identity between this gene and its closest published counterparts is lower than 60%. The phytase was named PhyRC001 and was biochemically characterized. This recombinant protein showed activity on sodium phytate, indicating that PhyRC001 is a hydrolase enzyme. The enzymatic activity was optimal at a pH of 7.0 and at a temperature of 35 °C. β-propeller phytases possess great potential as feed additives because they are the only type of phytase with high activity at neutral pH. Therefore, to explore and exploit the underlying mechanism for β-propeller phytase functions could be of great benefit to biotechnology.

Keywords: crop residues; functional metagenomics; phytasic activity.

MeSH terms

  • 6-Phytase / antagonists & inhibitors
  • 6-Phytase / chemistry
  • 6-Phytase / genetics*
  • Amino Acid Sequence
  • Bacteria / enzymology*
  • Bacteria / genetics
  • Environment
  • Enzyme Stability / drug effects
  • Gene Library
  • Genes, Bacterial
  • Hydrogen-Ion Concentration
  • Ions
  • Metagenomics*
  • Metals / pharmacology
  • Models, Molecular
  • Phylogeny
  • Recombinant Proteins / isolation & purification
  • Sequence Analysis, DNA
  • Structural Homology, Protein
  • Substrate Specificity / drug effects
  • Temperature

Substances

  • Ions
  • Metals
  • Recombinant Proteins
  • 6-Phytase