Bioinformatics Analysis of Upstream Region and Protein Structure of Fungal Phytase Gene


M. Gholizade 1 , * , M. R. Nassiry 2 , M. R. Saberi 3 , A. A. Haddad-Mashadrizeh 4

1 Department of Animal Sciences, Faculty of Animal and Food Sciences, Khuzestan Ramin Agriculture and Natural Resources University, Mollasani, Ahvaz, Iran

2 Department of Genetics, Faculty of Animal Sciences, Ferdowsi University of Mashhad, Mashhad, Iran

3 Department of Medical Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

4 Cell and Molecular Biotechnology Research Group, Institute of Biotechnology, Ferdowsi University of Mashhad, Mashhad, Iran

How to Cite: Gholizade M, Nassiry M R , Saberi M R, Haddad-Mashadrizeh A A . Bioinformatics Analysis of Upstream Region and Protein Structure of Fungal Phytase Gene, Arch Razi Inst. 2018 ; 73(3):e84913. doi: 10.22092/ari.2017.109655.1115.


Archives of Razi Institute: 73 (3); 229-237
Published Online: September 01, 2018
Article Type: Observational Study
Received: February 17, 2017
Accepted: July 07, 2017


Phytase increases the bioavailability of phytate phosphorus in seed-based animal feeds and reduces the phosphorus pollution of animal waste. Since most animal feeds for pellets are heated up to 65-80 °C, the production of a thermostable structure for phytase can be useful. In this study, we sought to perform bioinformatics analysis of the upstream region and protein structure of fungal phytase to improve its expression and thermostability properties. We used bioinformatics methods such as similarity search, multiple alignment, statistical analysis of physicochemical properties of amino acids, pattern recognition, and protein modeling to find out the effective factors in heat resistance of phytase. Change in Gibbs free energy (ΔG) of the best pattern promoter resulting from the interaction between RNA polymerase and the promoter sequences of modified genes of phytase was equal to -9 kcalmol-1, which is lower compared to other interactions. The evaluation of the three-dimensional structure of new phytases showed that amino acid substitutions aimed at improving thermostability did not change the form and structure of the protein. The results of Prochek, Whatcheck, and ERRAT for structural analysis and verification were 84, 72, and 70, respectively, that were satisfactory.


© 2018, Author(s). Razi Vaccine and Serum Research Institute.