Genome-Scale Characterization of Fungal Phytases and a Comparative Study Between Beta-Propeller Phytases and Histidine A
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Genome-Scale Characterization of Fungal Phytases and a Comparative Study Between Beta-Propeller Phytases and Histidine Acid Phosphatases Roberta Corsino Ferreira 1 & Murillo Peterlini Tavares 1 & Túlio Morgan 1 & Yan da Silva Clevelares 1 & Marina Quádrio Raposo Branco Rodrigues 1 & Maria Catarina Megumi Kasuya 2 & Tiago Antônio de Oliveira Mendes 1 & Valéria Monteze Guimarães 1 Received: 8 October 2019 / Accepted: 12 March 2020/ # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract
This work intended to prospect new phytase-producing organisms. In silico genomic analyses allowed the selection of twelve potential phytase-producing fungi. Based on gene sequence, it was possible to identify four well-defined groups of phytate-degrading enzymes: esterase-like, β-propeller phytases (βPP), phosphoglycerate mutase-like, and phytases of the histidine acid phosphatases (HAP) family. Analysis of the predicted genes encoding phytases belonging to the HAP family and βPP phytases and in silico characterization of these enzymes indicated divergence among the catalytic activities. Predicted fungal βPP phytases exhibited higher molecular mass (around 77 kDa) probably due to the epidermal growth factor-like domain. Twelve sequences of phytases contained signal peptides, of which seven were classified as HAP and five as βPP phytases, while ten sequences were predicted as phytases secreted by non-classical pathways. These fungi were grown in liquid or semi-solid medium, and the fungal enzymatic extracts were evaluated for their ability to hydrolyze sodium phytate at 50 °C and pH ranging from 2.0 to 9.0. Seven fungi were identified as phytase producers based on phosphate release under enzyme assay conditions. Results obtained from in silico analyses combining experimental enzymatic activities suggest that some selected fungi could secrete βPP phytases and HAP phytases. Keywords Fungi . Histidine acid phosphatases . Beta-propeller phytases . In silico characterization . Phytase activity
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12010-02003309-7) contains supplementary material, which is available to authorized users.
* Valéria Monteze Guimarães [email protected] Extended author information available on the last page of the article
Applied Biochemistry and Biotechnology
Introduction Phytic acid (myo-inositol 1, 2, 3, 4, 5, 6-hexaphosphate dihydrogenphosphate) and its respective salts known as phytates are formed by a myo-inositol ring with six phosphatelinked groups [1, 2]. Phytic acid is the predominant form of phosphorus storage by plants, especially cereals, oil seeds, and legumes [3]. Non-ruminant animals, including humans, are unable to hydrolyze phytic acid due to the absence of phytases in the digestive tract. Therefore, phytic acid is considered an antinutritional factor for these animals, since it may act as a chelating agent and bind to cations such as Ca2+, Mg+2, Zn+2, Fe+2, Cu+2, Cu+, and K+, affecting the uptake and digestion of minerals [2].
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