Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Farias, Nathálya, Almeida, Isabela, Meneses, Carlos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
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
_version_ 1783334744091525120
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
work_keys_str_mv AT fariasnathalya newbacterialphytasethroughmetagenomicprospection
AT almeidaisabela newbacterialphytasethroughmetagenomicprospection
AT menesescarlos newbacterialphytasethroughmetagenomicprospection