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

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.

journal_name

FEMS Microbiol Lett

authors

Tkachenko AA,Kalinina AN,Borshchevskaya LN,Sineoky SP,Gordeeva TL

doi

10.1093/femsle/fnaa217

subject

Has Abstract

pub_date

2020-12-21 00:00:00

eissn

0378-1097

issn

1574-6968

pii

6043202

pub_type

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