A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing

Abstract Phytases are widely utilized in feed industry to increase the utilization of phosphorus, minerals, and amino acids for improvement of animal and human nutrition. At present, all known β-propeller phytases (BPP) have been generated from bacteria, particularly Bacillus. In this work we report...

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Main Authors: Xianjuan Hou, Zhen Shen, Na Li, Xiaowei Kong, Kangliang Sheng, Jingmin Wang, Yongzhong Wang
Format: Article
Language:English
Published: BMC 2020-04-01
Series:Microbial Cell Factories
Subjects:
Online Access:http://link.springer.com/article/10.1186/s12934-020-01346-9
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spelling doaj-419d9b4d026b426290b9f80c37ae67982020-11-25T02:04:14ZengBMCMicrobial Cell Factories1475-28592020-04-0119111310.1186/s12934-020-01346-9A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processingXianjuan Hou0Zhen Shen1Na Li2Xiaowei Kong3Kangliang Sheng4Jingmin Wang5Yongzhong Wang6School of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversitySchool of Life Sciences, Anhui UniversityAbstract Phytases are widely utilized in feed industry to increase the utilization of phosphorus, minerals, and amino acids for improvement of animal and human nutrition. At present, all known β-propeller phytases (BPP) have been generated from bacteria, particularly Bacillus. In this work we report for the first time a new fungal-derived BPP phytase. We identified a phytase highly differentially expressed only in the parasitic stage of a nematophagous fungus, Arhtrobotrys oliogospora, during the development of the 3D traps. We found that this phytase was homologous to the known bacterial BPP phytase, thus we referred the new phytase to Aophytase. The heterologous expression of codon-optimized Aophytase gene in Pichia pastoris was successfully investigated to yield recombinant Aophytase (r-Aophytase) with high specific enzyme activity of 74.71 U/mg, much higher than those of recombinant BPP phytases derived bacteria. The kinetic parameters of the r-Aophytase, the optimum pH and temperature, as well as the effects of surfactant, EDTA and different ions on its enzyme activity were further investigated. The potential utilization of r-Aophytase in feed processing was finally explored. We found that the optimal pH value was about 7.5, and the optimal temperature was 50 °C.; r-Aophytase significantly increased the release of inorganic phosphorus from soybean meal, and improved the release of soluble minerals from the durum wheat flour and finger millet flour. The findings indicate its potential utilization in the feed processing to ameliorate nutritional value of cereals and animal feed in the future.http://link.springer.com/article/10.1186/s12934-020-01346-9Nematophagous fungiArthrobotrys oligosporaPhytasePhosphorus and mineral releaseFeed processing
collection DOAJ
language English
format Article
sources DOAJ
author Xianjuan Hou
Zhen Shen
Na Li
Xiaowei Kong
Kangliang Sheng
Jingmin Wang
Yongzhong Wang
spellingShingle Xianjuan Hou
Zhen Shen
Na Li
Xiaowei Kong
Kangliang Sheng
Jingmin Wang
Yongzhong Wang
A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
Microbial Cell Factories
Nematophagous fungi
Arthrobotrys oligospora
Phytase
Phosphorus and mineral release
Feed processing
author_facet Xianjuan Hou
Zhen Shen
Na Li
Xiaowei Kong
Kangliang Sheng
Jingmin Wang
Yongzhong Wang
author_sort Xianjuan Hou
title A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
title_short A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
title_full A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
title_fullStr A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
title_full_unstemmed A novel fungal beta-propeller phytase from nematophagous Arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
title_sort novel fungal beta-propeller phytase from nematophagous arthrobotrys oligospora: characterization and potential application in phosphorus and mineral release for feed processing
publisher BMC
series Microbial Cell Factories
issn 1475-2859
publishDate 2020-04-01
description Abstract Phytases are widely utilized in feed industry to increase the utilization of phosphorus, minerals, and amino acids for improvement of animal and human nutrition. At present, all known β-propeller phytases (BPP) have been generated from bacteria, particularly Bacillus. In this work we report for the first time a new fungal-derived BPP phytase. We identified a phytase highly differentially expressed only in the parasitic stage of a nematophagous fungus, Arhtrobotrys oliogospora, during the development of the 3D traps. We found that this phytase was homologous to the known bacterial BPP phytase, thus we referred the new phytase to Aophytase. The heterologous expression of codon-optimized Aophytase gene in Pichia pastoris was successfully investigated to yield recombinant Aophytase (r-Aophytase) with high specific enzyme activity of 74.71 U/mg, much higher than those of recombinant BPP phytases derived bacteria. The kinetic parameters of the r-Aophytase, the optimum pH and temperature, as well as the effects of surfactant, EDTA and different ions on its enzyme activity were further investigated. The potential utilization of r-Aophytase in feed processing was finally explored. We found that the optimal pH value was about 7.5, and the optimal temperature was 50 °C.; r-Aophytase significantly increased the release of inorganic phosphorus from soybean meal, and improved the release of soluble minerals from the durum wheat flour and finger millet flour. The findings indicate its potential utilization in the feed processing to ameliorate nutritional value of cereals and animal feed in the future.
topic Nematophagous fungi
Arthrobotrys oligospora
Phytase
Phosphorus and mineral release
Feed processing
url http://link.springer.com/article/10.1186/s12934-020-01346-9
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