Enhancing thermal tolerance of Aspergillus niger PhyA phytase directed by structural comparison and computational simulation.

ABSTRACT:

Background

Phytase supplied in feeds for monogastric animals is important for improving nutrient uptake and reducing phosphorous pollution. High-thermostability phytases are particularly desirable due to their ability to withstand transient high temperatures during feed pelleting procedures. A comparison of crystal structures of the widely used industrial Aspergillus niger PhyA phytase (AnP) with its close homolog, the thermostable Aspergillus fumigatus phytase (AfP), suggests 18 residues in three segments associated with thermostability. In this work, we aim to improve the thermostability of AnP through site-directed mutagenesis. We identified favorable mutations based on structural comparison of homologous phytases and molecular dynamics simulations.

Results

A recombinant

SUBMITTER: Han N 

PROVIDER: S-EPMC5984770 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature