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Computational-based structural, functional and phylogenetic analysis of Enterobacter phytases.

Krishnendu Pramanik1, Shreyasi Kundu1, Sandipan Banerjee1

  • 1Microbiology Laboratory, Department of Botany, The University of Burdwan, Purba Bardhaman, West Bengal 713104 India.

3 Biotech
|May 29, 2018
PubMed
Summary

Bio-computational analysis of Enterobacter phytases reveals acidic, thermostable enzymes with high alpha-helical content. These histidine acid phosphatases, featuring conserved DG-DP-LG residues, are suitable as food additives in the animal industry.

Keywords:
Acidic phytasesEnterobacter spp.Histidine phosphatase superfamilyIn silico analysisMyo-inositol hexakisphosphate phosphohydrolasesThermostable

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinformatics

Background:

  • Myo-inositol hexakisphosphate phosphohydrolases, or phytases, are crucial enzymes for solubilizing insoluble phosphates.
  • Enterobacter species are a potential source of industrially relevant phytases.

Purpose of the Study:

  • To characterize Enterobacter phytases using bio-computational tools.
  • To evaluate their suitability as food additives for the animal industry.

Main Methods:

  • Phylogenetic, structural, and functional analysis using bio-computational tools.
  • Prediction of isoelectric points, aliphatic indices, molecular weight, and GRAVY scores.
  • Secondary and tertiary structure prediction, including 3D model deposition.
  • Functional analysis and multiple sequence alignment to identify conserved residues.

Main Results:

  • Enterobacter phytases are predominantly acidic (pI < 7.0) and possess thermostable characteristics (aliphatic index < 40).
  • Average molecular weight is 48 kDa, with low GRAVY scores indicating good water interaction.
  • Secondary structure analysis shows a high proportion of alpha-helical content.
  • Tertiary structure prediction reveals tetrameric proteins, with the E. aerogenes model deposited in the Protein Model Database.
  • Functional analysis confirms classification as histidine acid phosphatases, with conserved DG-DP-LG residues identified.

Conclusions:

  • Enterobacter phytases exhibit favorable biochemical and structural properties for industrial applications.
  • The conserved residues and structural features suggest their potential as effective phytase-producing microbes for animal feed additives.