Screening and Characterization of Phytases from Bacteria Isolated from Chilean Hydrothermal Environments

Milko A Jorquera; Stefanie Gabler; Nitza G Inostroza; Jacquelinne J Acuña; Marco A Campos; Daniel Menezes-Blackburn; Ralf Greiner

doi:10.1007/s00248-017-1057-0

Screening and Characterization of Phytases from Bacteria Isolated from Chilean Hydrothermal Environments

Milko A Jorquera, Stefanie Gabler, Nitza G Inostroza, Jacquelinne J Acuña, Marco A Campos, Daniel Menezes-Blackburn, Ralf Greiner

Soils, Water and Agricultural Engineering

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

Abstract

Phytases are enzymes involved in organic phosphorus cycling in nature and widely used as feed additives in animal diets. Thermal tolerance is a desired property of phytases. The objectives of this study were to screen and characterize bacterial phytases from Chilean hydrothermal environments. In this study, 60% (30 of 63) of screened thermophilic (60 °C) isolates showed phytase activity in crude protein extracts. The characterization of phytase from two selected isolates (9B and 15C) revealed that both isolates produce phytases with a pH optimum at 5.0. The temperature optimum for phytate dephosphorylation was determined to be 60 and 50 °C for the phytases from the isolates 9B and 15C, respectively. Interestingly, the phytase from the isolate 15C showed a residual activity of 46% after incubation at 90 °C for 20 min. The stepwise dephosphorylation of phytate by protein extracts of the isolates 9B and 15C was verified by HLPC analysis. Finally, the isolates 9B and 15C were identified by partial sequencing of the 16S rRNA gene as members of the genera Bacillus and Geobacillus, respectively.

Original language	English
Pages (from-to)	387-399
Number of pages	13
Journal	Microbial Ecology
Volume	75
Issue number	2
DOIs	https://doi.org/10.1007/s00248-017-1057-0
Publication status	Published - Feb 1 2018

Keywords

6-Phytase/chemistry
Bacteria/classification
Bacterial Proteins/chemistry
Enzyme Stability
Hydrogen-Ion Concentration
Hydrothermal Vents/microbiology
Kinetics
Temperature

ASJC Scopus subject areas

Ecology, Evolution, Behavior and Systematics
Ecology
Soil Science

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10.1007/s00248-017-1057-0

Cite this

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title = "Screening and Characterization of Phytases from Bacteria Isolated from Chilean Hydrothermal Environments",

abstract = "Phytases are enzymes involved in organic phosphorus cycling in nature and widely used as feed additives in animal diets. Thermal tolerance is a desired property of phytases. The objectives of this study were to screen and characterize bacterial phytases from Chilean hydrothermal environments. In this study, 60% (30 of 63) of screened thermophilic (60 °C) isolates showed phytase activity in crude protein extracts. The characterization of phytase from two selected isolates (9B and 15C) revealed that both isolates produce phytases with a pH optimum at 5.0. The temperature optimum for phytate dephosphorylation was determined to be 60 and 50 °C for the phytases from the isolates 9B and 15C, respectively. Interestingly, the phytase from the isolate 15C showed a residual activity of 46% after incubation at 90 °C for 20 min. The stepwise dephosphorylation of phytate by protein extracts of the isolates 9B and 15C was verified by HLPC analysis. Finally, the isolates 9B and 15C were identified by partial sequencing of the 16S rRNA gene as members of the genera Bacillus and Geobacillus, respectively.",

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AU - Jorquera, Milko A

AU - Gabler, Stefanie

AU - Inostroza, Nitza G

AU - Acuña, Jacquelinne J

AU - Campos, Marco A

AU - Menezes-Blackburn, Daniel

AU - Greiner, Ralf

PY - 2018/2/1

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N2 - Phytases are enzymes involved in organic phosphorus cycling in nature and widely used as feed additives in animal diets. Thermal tolerance is a desired property of phytases. The objectives of this study were to screen and characterize bacterial phytases from Chilean hydrothermal environments. In this study, 60% (30 of 63) of screened thermophilic (60 °C) isolates showed phytase activity in crude protein extracts. The characterization of phytase from two selected isolates (9B and 15C) revealed that both isolates produce phytases with a pH optimum at 5.0. The temperature optimum for phytate dephosphorylation was determined to be 60 and 50 °C for the phytases from the isolates 9B and 15C, respectively. Interestingly, the phytase from the isolate 15C showed a residual activity of 46% after incubation at 90 °C for 20 min. The stepwise dephosphorylation of phytate by protein extracts of the isolates 9B and 15C was verified by HLPC analysis. Finally, the isolates 9B and 15C were identified by partial sequencing of the 16S rRNA gene as members of the genera Bacillus and Geobacillus, respectively.

AB - Phytases are enzymes involved in organic phosphorus cycling in nature and widely used as feed additives in animal diets. Thermal tolerance is a desired property of phytases. The objectives of this study were to screen and characterize bacterial phytases from Chilean hydrothermal environments. In this study, 60% (30 of 63) of screened thermophilic (60 °C) isolates showed phytase activity in crude protein extracts. The characterization of phytase from two selected isolates (9B and 15C) revealed that both isolates produce phytases with a pH optimum at 5.0. The temperature optimum for phytate dephosphorylation was determined to be 60 and 50 °C for the phytases from the isolates 9B and 15C, respectively. Interestingly, the phytase from the isolate 15C showed a residual activity of 46% after incubation at 90 °C for 20 min. The stepwise dephosphorylation of phytate by protein extracts of the isolates 9B and 15C was verified by HLPC analysis. Finally, the isolates 9B and 15C were identified by partial sequencing of the 16S rRNA gene as members of the genera Bacillus and Geobacillus, respectively.

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KW - Bacterial Proteins/chemistry

KW - Enzyme Stability

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KW - Kinetics

KW - Temperature

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Screening and Characterization of Phytases from Bacteria Isolated from Chilean Hydrothermal Environments

Abstract

Keywords

ASJC Scopus subject areas

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