phytase/atrofiere

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Molecular cloning of a phytase gene (phy M) from Pseudomonas syringae MOK1.

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A phytase gene (phy M) was cloned from Pseudomonas syringae MOK1 by two steps of degenerate PCR and inverse PCR. This gene consists of 1,287 nucleotides and encodes a polypeptide of 428 amino acids with a deduced molecular mass of 46,652 kDa. Based on its amino acid sequence, the Phy M shares the

A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris.

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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 (TAIL) PCR and was overexpressed in Pichia pastoris. Sequence analysis revealed one open reading

Novel low-temperature-active phytase from Erwinia carotovora var.carotovota ACCC 10276.

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A phytase with high activity at low temperatures has great potential for feed applications, especially in aquaculture. Therefore, this study used a degenerate PCR and TAIL PCR to clone a phytase gene from Erwinia carotovora var. carotovota, the cause of soft rot of vegetables in the ground or during

Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger.

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Phytase catalyzes the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. A gene (phyA) of Aspergillus niger NRRL3135 coding for extracellular, glycosylated phytase was isolated using degenerate oligodeoxyribonucleotides deduced from phytase amino acid (aa)

Molecular cloning of the phytase gene from Citrobacter braakii and its expression in Saccharomyces cerevisiae.

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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 sequence of the phytase. The deduced amino acid sequence of appA contained the N-terminal RHGXRXP motif

Cloning, expression, and characterization of a new phytase from the phytopathogenic bacterium Pectobacterium wasabiae DSMZ 18074.

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The soft rot bacterium Pectobacterium wasabiae is an economically important pathogen of many crops. A new phytase gene, appA, was cloned from P. wasabiae by degenerate PCR and TAIL-PCR. The open reading frame of appA consisted of 1,302 bp encoding 433 amino acid residues, including 27 residues of a

A novel phytase with preferable characteristics from Yersinia intermedia.

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A Yersinia intermedia strain producing phytase was isolated from glacier soil. The phytase gene, appA, was isolated by degenerate PCR and TAIL-PCR. The full-length fragment contained 2354bp with a 1326-bp open reading frame encoding 441 amino acids. APPA contained the active site RHGXRXP and HD

Gene cloning, expression, and characterization of a novel phytase from Dickeya paradisiaca.

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A novel phytase gene, appA, was isolated by degenerate polymerase chain reaction (PCR) and thermal asymmetric interlaced PCR from Dickeya paradisiaca. The full-length appA comprises 1278 bp and encodes 425 amino acid residues, including a 23-residue putative N-terminal signal peptide. The deduced

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

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A phytase with high activity at neutral pH and typical water temperatures ( approximately 25 degrees C) could effectively hydrolyze phytate in aquaculture. In this study, a phytase-producing strain, Pedobacter nyackensis MJ11 CGMCC 2503, was isolated from glacier soil, and the relevant gene, PhyP,

Purification, sequencing and evaluation of a divergent phytase from Penicillium oxalicum KCTC6440.

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A fungal strain producing high levels of phytase was purified to homogeneity from Penicillium oxalicum KCTC6440 (PhyA). The molecular mass of the purified PhyA was 65 kDa and optimal activity occurred at 55°C. The enzyme was stable in a pH range of 4.5-6.5, with an optimum performance at pH 5.5. The

Diversity of phytases in the rumen.

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Examples of a new class of phytase related to protein tyrosine phosphatases (PTP) were recently isolated from several anaerobic bacteria from the rumen of cattle. In this study, the diversity of PTP-like phytase gene sequences in the rumen was surveyed by using the polymerase chain reaction (PCR).

Pphy--a cell-bound phytase from the yeast Pichia anomala: molecular cloning of the gene PPHY and characterization of the recombinant enzyme.

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The Pichia anomala gene PPHY, which codes for a cell-bound phytase, was isolated from genomic DNA by PCR, using oligonucleotide sequences derived from the N-terminal region of the purified phytase protein (Pphyp) and a degenerate primer derived from conserved sequences of yeast and fungal phytases

Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis.

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A novel phytase gene ( phyL) was cloned from Bacillus licheniformis by multiple steps of degenerate and inverse PCR. The coding region of the phyL gene was 1,146 bp in size and a promoter region of approximately 300 bp was identified at the upstream sequence. This gene, together with a phytase gene

Characterization of phosphate accumulation in Lolium multiflorum for remediation of phosphorus-enriched soils.

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Deterioration in water quality caused by the movement of excessive soil P has created a condition necessary for the development of a sustainable P remediation technology. In this investigation, the phytoremediation potential of Gulf and Marshall ryegrass (Lolium multiflorum) grown in a greenhouse

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