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

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...

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Bibliographic Details
Published in:FEMS microbiology letters 2021-01, Vol.368 (2), p.1
Main Authors: Tkachenko, Artur A, Kalinina, Anna N, Borshchevskaya, Larisa N, Sineoky, Sergey P, Gordeeva, Tatiana L
Format: Article
Language:English
Subjects:
Chemical synthesis
DNA sequencing
Enzymes
Genes
Genetic aspects
Identification and classification
Methods
Methylotrophs
Nucleotide sequencing
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Summary: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[degrees]C, respectively. The specific activity of the enzyme was 1577 U/mg. The Michaelis constant ([K.sub.m]) and the maximum reaction rate ([V.sub.max]) 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.
ISSN:1574-6968
0378-1097
1574-6968
DOI:10.1093/femsle/fnaa217