A novel phytase from Citrobacter gillenii: characterization and expression in Pichia pastoris (Komagataella pastoris) | Zendy

A. A. Tkachenko | Zendy; A. N. Kalinina | Zendy; L. N. Borshchevskaya | Zendy; S. P. Sineoky | Zendy; T. L. Gordeeva | Zendy

Open Access

A novel phytase from Citrobacter gillenii: characterization and expression in Pichia pastoris (Komagataella pastoris)

Author(s) -

A. A. Tkachenko,

A. N. Kalinina,

L. N. Borshchevskaya,

S. P. Sineoky,

T. L. Gordeeva

Publication year - 2020

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.899

H-Index - 151

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1093/femsle/fnaa217

Subject(s) - pichia pastoris , phytase , biochemistry , histidine , citrobacter , peptide sequence , enzyme , michaelis–menten kinetics , biology , enzyme kinetics , amino acid , chemistry , recombinant dna , microbiology and biotechnology , enzyme assay , escherichia coli , gene , active site , enterobacteriaceae

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.

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