A novel phytase with preferable characteristics from Yersinia intermedia.

  title={A novel phytase with preferable characteristics from Yersinia intermedia.},
  author={Huo-qing Huang and Huiying Luo and Peilong Yang and Kun Meng and Yaru Wang and Tie-zheng Yuan and Yingguo Bai and Bin Yao},
  journal={Biochemical and biophysical research communications},
  volume={350 4},

Gene Cloning, Expression, and Characterization of a Novel Phytase from Dickeya paradisiaca

The deduced amino acid sequence of appA reveals the conserved motifs RHGXRXP and HD, which are typical of histidine acid phosphatases; significantly, APPA shows maximum identity (49%) to a phytase from Klebsiella pneumoniae.

A Novel Phytase appA from Citrobacter amalonaticus CGMCC 1696: Gene Cloning and Overexpression in Pichia pastoris

A novel phytase gene appA, with upstream and downstream sequences from Citrobacter amalonaticus CGMCC 1696, was cloned by degenerate polymerase chain reaction (PCR), and thermal asymmetric interlaced

Expression and biochemical characterization of a Yersinia intermedia phytase expressed in Escherichia coli.

The biochemical properties of the rPHY could be usefull in future for its industrial application of this enzyme as an additive in monogastric feed and for this reason, them were protected by Intelllectual Property Law in Brazil.

New Recombinant Phytase from Kosakonia sacchari: characteristic and biotechnological potential

It was shown that the enzyme was characterized by a wide range of working pH, and the properties of a new recombinant phytase allow us to consider it as a high-potential enzyme for agrobiotechnology.

Improvement of Yersinia frederiksenii phytase performance by a single amino acid substitution

A previously unrecognized factor other than electrostatics—presumably the side‐chain structure near the active site—contributes to the optimal pH for APPA activity, making S51T a better candidate than the wild‐type APPA for use in animal feed.

A novel phytase from Yersinia rohdei with high phytate hydrolysis activity under low pH and strong pepsin conditions

This study indicated that, in order to better hydrolyze the phytate and release more inorganic phosphorus in the gastric passage, phytase should have high activity and stability, simultaneously, at low pH and high protease concentration.

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

The phyCg gene encoding a new phytase from C. gillenii was optimized, synthesized, cloned, and expressed in Pichia pastoris and showed the pH and trypsin stability and had a high activity over a wide pH range.

Purification, biochemical characterization, and genetic cloning of the phytase produced by Burkholderia sp. strain a13.

A phytase-producing bacterium, Burkholderia sp. a13 (JCM 30421), was isolated from Lake Kasumigaura by enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus

A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive

R-PhyP had higher relative activity at 25°C, and hydrolyzed phytate from soybean with greater efficacy at neutral pH, and might be a good candidate for an aquatic feed additive in the aquaculture industry.

Cloning, Codon Optimization, and Expression of Yersinia intermedia Phytase Gene in E. coli.

The results of the expression and enzyme characterization revealed that the optimized Y. intermedia phytase gene has a good potential to be produced commercially and to be applied in animals' foods industryry.



Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1

The phytase protein was purified and characterised as a 42 kDa protein accepting phytate, NADP and sugar phosphates as substrates, and the corresponding gene (phyK) was cloned from chromosomal DNA using a combined approach of protein and genome analysis and expressed in Escherichia coli.

Molecular Cloning of the Phytase Gene from Citrobacter  braakii and its Expression in Saccharomyces cerevisiae

The gene, appA, encoding phytase was cloned from a size-selected genomic library of Citrobacter  braakii YH-15 by Southern hybridization using a degenerate probe based on the N-terminal amino acid

Isolation and characterization of a phytase with improved properties from Citrobacter braakii

Citrobacter braakii YH-15 produced an intracellular phytase which was purified 12 800 fold to homogeneity with the specific activity of 3 457 units mg−1, which is 1.9 times higher than E. coli

High level expression of a synthetic gene encoding Peniophora lycii phytase in methylotrophic yeast Pichia pastoris

The gene constructs containing wild type or modified phytase gene coding sequences under the control of the highly-inducible alcohol oxidase gene (AOX1) promoter, the synthetic signal peptide (designated MF4I), which is a codon-modified Saccharomyces cerevisiae mating factor α-prepro-leader sequence, were used to transform P. pastoris.

Biochemical Characterization of Fungal Phytases (myo-Inositol Hexakisphosphate Phosphohydrolases): Catalytic Properties

To extend the biochemical characterization of wild-type phytases, the catalytic properties of a series of fungal phytased, as well as Escherichia coli phytase, were determined and phosphate liberation kinetics were studied in vitro.

[Overexpression of Escherchia coli phytase with high specific activity].

The gene appA encoding Escherchia coli phytase AppA with high specific activity was modified and artificially synthesized according to the bias in codon choice of the high expression gene in Pichia pastoris without changing the amino acid sequence of the AppA.

Comparative studies on the in vitro properties of phytases from various microbial origins

It can be concluded that phytases of various microbial origins behave differently with respect to their in vitro properties which could be of importance for future developments of phytase preparations.

[Overexpression of artificial synthetic gene of Aspergillus niger NRRL3135 phytase in Pichia pastoris].

After screening for high level productive yeast strains, a strain named SPAN-III produced recombinant phytase with 165,000 u/mL under the condition of shake cultivation, which will satisfy the demand for industrialized production in some degree.