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A novel phytase from Citrobactergillenii: characterization and expression in Pichia pastoris (Komagataella pastoris).

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Title: A novel phytase from Citrobactergillenii: characterization and expression in Pichia pastoris (Komagataella pastoris).
Authors: Tkachenko, Artur A1 (AUTHOR) artur.tka4enko10@gmail.com, Kalinina, Anna N2 (AUTHOR), Borshchevskaya, Larisa N2 (AUTHOR), Sineoky, Sergey P2 (AUTHOR), Gordeeva, Tatiana L1,2 (AUTHOR)
Source: FEMS Microbiology Letters. 1/15/2021, Vol. 368 Issue 2, p1-1. 1p.
Subjects: Pichia pastoris, Amino acid sequence, Phytases, Acid phosphatase
Abstract: The phyCg gene encoding a new phytase from Citrobacter gillenii was optimized, synthesized, cloned and expressed in Pichia pastoris. Analysis of the amino acid sequence of the enzyme showed that it belongs to the histidine acid phosphatase family. The amino acid sequence of the PhyCg phytase has the highest homology (73.49%) with a phytase sequence from Citrobacter braakii. The main characteristics for the purified recombinant phytase were established. The optimum pH and temperature were 4.5 and 50°C, respectively. The specific activity of the enzyme was 1577 U/mg. The Michaelis constant (Km) and the maximum reaction rate (Vmax) for sodium phytate were 0.185 mM and 2185 U/mg, respectively. The enzyme showed the pH and trypsin stability and had a high activity over a wide pH range. [ABSTRACT FROM AUTHOR]
Copyright of FEMS Microbiology Letters is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: A novel phytase from Citrobactergillenii: characterization and expression in Pichia pastoris (Komagataella pastoris).
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  Data: <searchLink fieldCode="AR" term="%22Tkachenko%2C+Artur+A%22">Tkachenko, Artur A</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> artur.tka4enko10@gmail.com</i><br /><searchLink fieldCode="AR" term="%22Kalinina%2C+Anna+N%22">Kalinina, Anna N</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Borshchevskaya%2C+Larisa+N%22">Borshchevskaya, Larisa N</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sineoky%2C+Sergey+P%22">Sineoky, Sergey P</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Gordeeva%2C+Tatiana+L%22">Gordeeva, Tatiana L</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22FEMS+Microbiology+Letters%22">FEMS Microbiology Letters</searchLink>. 1/15/2021, Vol. 368 Issue 2, p1-1. 1p.
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  Data: <searchLink fieldCode="DE" term="%22Pichia+pastoris%22">Pichia pastoris</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+acid+sequence%22">Amino acid sequence</searchLink><br /><searchLink fieldCode="DE" term="%22Phytases%22">Phytases</searchLink><br /><searchLink fieldCode="DE" term="%22Acid+phosphatase%22">Acid phosphatase</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The phyCg gene encoding a new phytase from Citrobacter gillenii was optimized, synthesized, cloned and expressed in Pichia pastoris. Analysis of the amino acid sequence of the enzyme showed that it belongs to the histidine acid phosphatase family. The amino acid sequence of the PhyCg phytase has the highest homology (73.49%) with a phytase sequence from Citrobacter braakii. The main characteristics for the purified recombinant phytase were established. The optimum pH and temperature were 4.5 and 50°C, respectively. The specific activity of the enzyme was 1577 U/mg. The Michaelis constant (Km) and the maximum reaction rate (Vmax) for sodium phytate were 0.185 mM and 2185 U/mg, respectively. The enzyme showed the pH and trypsin stability and had a high activity over a wide pH range. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of FEMS Microbiology Letters is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1093/femsle/fnaa217
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        Text: English
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        Type: general
      – SubjectFull: Amino acid sequence
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      – SubjectFull: Phytases
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      – SubjectFull: Acid phosphatase
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              Text: 1/15/2021
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