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New Bacterial Phytase through Metagenomic Prospection
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 microor...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6017413/ https://www.ncbi.nlm.nih.gov/pubmed/29462992 http://dx.doi.org/10.3390/molecules23020448 |
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author | Farias, Nathálya Almeida, Isabela Meneses, Carlos |
author_facet | Farias, Nathálya Almeida, Isabela Meneses, Carlos |
author_sort | Farias, Nathálya |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6017413 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-60174132018-11-13 New Bacterial Phytase through Metagenomic Prospection Farias, Nathálya Almeida, Isabela Meneses, Carlos Molecules Article 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. MDPI 2018-02-17 /pmc/articles/PMC6017413/ /pubmed/29462992 http://dx.doi.org/10.3390/molecules23020448 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Farias, Nathálya Almeida, Isabela Meneses, Carlos New Bacterial Phytase through Metagenomic Prospection |
title | New Bacterial Phytase through Metagenomic Prospection |
title_full | New Bacterial Phytase through Metagenomic Prospection |
title_fullStr | New Bacterial Phytase through Metagenomic Prospection |
title_full_unstemmed | New Bacterial Phytase through Metagenomic Prospection |
title_short | New Bacterial Phytase through Metagenomic Prospection |
title_sort | new bacterial phytase through metagenomic prospection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6017413/ https://www.ncbi.nlm.nih.gov/pubmed/29462992 http://dx.doi.org/10.3390/molecules23020448 |
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