Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.8 (phytase)
1,997 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two studies were conducted to determine the efficacy of an Escherichia coli-derived phytase (ECP) and its equivalency relative to inorganic phosphorus (iP) from monosodium phosphate (MSP). In Exp. 1, one thousand two hundred 1-d-old male broilers were used in a 42-d trial to assess the effect of ECP and iP supplementation on growth performance and nutrient digestibility. Dietary treatments were based on corn-soybean meal basal diets (BD) containing 239 and 221 g of CP, 8.2 and 6.6 g of Ca, and 2.4 and 1.5 g of nonphytate P (nPP) per kg for the starter and grower phases, respectively. Treatments consisted of the BD; the BD + 0.6, 1.2, or 1.8 g of iP from MSP per kg; and the BD + 250, 500, 750, or 1,000 phytase units (FTU) of ECP per kg. Increasing levels of MSP improved gain, gain:feed, and tibia ash (linear, P < 0.01). Increasing levels of ECP improved gain, gain:feed, tibia ash (linear, P < 0.01), apparent ileal digestibility of P, N, Arg, His, Phe, and Trp at d 21 (linear, P < 0.05), and apparent retention of P at d 21 (linear, P < 0.05). Increasing levels of ECP decreased apparent retention of energy (linear, P < 0.01). Five hundred FTU of ECP per kg was determined to be equivalent to the addition of 0.72, 0.78, and 1.19 g of iP from MSP per kg in broiler diets based on gain, feed intake, and bone ash, respectively. In Exp. 2, forty-eight 10-kg pigs were used in a 28-d trial to assess the effect of ECP and iP supplementation on growth performance and nutrient digestibility. Dietary treatments consisted of a positive control containing 6.1 and 3.5 g of Ca and nPP, respectively, per kg; a negative control (NC) containing 4.8 and 1.7 g of Ca and nPP, respectively, per kg; the NC diet plus 0.4, 0.8, or 1.2 g of iP from MSP per kg; and the NC diet plus 500, 750, or 1,000 FTU of ECP per kg. Daily gain improved (linear, P < 0.05) with ECP addition, as did apparent digestibility of Ca and P (linear, P < 0.01). Five hundred FTU of ECP per kg was determined to be equivalent to the addition of 0.49 and 1.00 g of iP from MSP per kg in starter pigs diets, based on ADG and bone ash, respectively.
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PMID:Efficacy and equivalency of an Escherichia coli-derived phytase for replacing inorganic phosphorus in the diets of broiler chickens and young pigs. 1709 29

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 putative signal peptide. The mature protein had a molecular mass of 45 kDa and a theoretical pI of 5.5. The amino acid sequence contained the conserved active site residues RHGXRXP and HDTN of typical histidine acid phosphatases, and showed the highest identity of 48.5% to PhyM from Pseudomonas syringae. The gene fragment encoding the mature phytase was expressed in Escherichia coli BL21 (DE3), and the purified recombinant phytase had a specific activity of 1,072+/-47 U/mg for phytate substrate. The optimum pH and temperature for the purified phytase were pH 5.0 and 50 degrees C, respectively. The Km value was 0.17 mM, with a Vmax of 1,714 micromol/min/mg. This is the first report of the identification and isolation of phytase from Pectobacterium.
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PMID:Cloning, expression, and characterization of a new phytase from the phytopathogenic bacterium Pectobacterium wasabiae DSMZ 18074. 1866 49

The extracellular phytase structural gene was isolated from the cDNA of the marine yeast, Kodamaea ohmeri BG3, using the switching mechanism at 5'-end of RNA transcript (SMART)trade mark rapid-amplification of cDNA ends (RACE) cDNA amplification kit. The gene had an open reading frame of 1389 bp and the coding region of the gene had no intron. It encoded 462 amino acid residues of a protein with a putative signal peptide of 15 amino acids. The protein sequence deduced from the extracellular phytase structural gene contained the consensus motifs (RHGXRX P and HD), which are conserved among histidine acid phosphatases, and six conserved putative N-glycosylation sites. According to the phylogenetic tree of the phytase, the phytase from K. ohmeri BG3 was closely related to Candida albicans (XP_713452) and Pichia stipitis (XP_001385108) phytase proteins and more distantly related to other phytases. The mature peptide encoding cDNA was subcloned into the pET-24a (+) expression vector. The recombinant plasmid [pET-24a (+)PHY1] was expressed in Escherichia coli BL21 (DE3). The expressed fusion protein was analysed by SDS-PAGE and Western blotting, and a specific band with a molecular mass of about 51 kDa was found. An enzyme activity assay verified the recombinant protein as a phytase. A maximum activity of 16.5 U mg(-1) was obtained from the cellular extract of E. coli BL21 (DE3) harbouring pET-24a (+)PHY1. The optimal pH and temperature of the crude recombinant lipase were 5 and 65 degrees C, respectively, and the crude recombinant phytase had hydrolytic activity towards phytate.
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PMID:Molecular cloning, characterization, and expression of the phytase gene from marine yeast Kodamaea ohmeri BG3. 1867 57

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 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. To characterize the properties of APPA, appA was expressed in Escherichia coli and purified. The purified recombinant APPA has two pH optima at pH 4.5 and 5.5, optimum temperature at 55 degrees C, specific activity of 769 U/mg, and good pH stability. The K(m) value for the substrate sodium phytate is 0.399 mM with a Vmax of 666 U/mg. To our knowledge, this is the first report of a phytase or phytase gene isolated from Dickeya.
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PMID:Gene cloning, expression, and characterization of a novel phytase from Dickeya paradisiaca. 1867 91

The effects of phytic acid and 2 sources of exogenous phytase (bacterial vs. fungal) on the flow of endogenous amino acids at the terminal ileum of broilers were assessed using the enzyme-hydrolyzed casein method. Phytic acid (as the sodium salt) was included in a purified diet at 8.5 and 14.5 g/kg, and each diet was fed without or with a fungal (Aspergillus niger-derived) or a bacterial (Escherichia coli-derived) microbial phytase at 500 phytase units/kg of diet. Increasing the concentration of phytic acid in the diet from 8.5 to 14.5 g/kg increased (P < 0.001) the flow of all measured amino acids by an average of 68%, with a range from 17% for proline to 145% for phenylalanine. The flow of endogenous aspartic acid, serine, glutamic acid, glycine, leucine, tyrosine, phenylalanine, and histidine were increased by more than the mean, indicating changes in the composition of endogenous protein in response to the presence of higher concentrations of phytic acid. Supplementation of both phytases reduced (P < 0.001) the flow of endogenous amino acids, but the reduction (P = 0.06) was greater for the bacterial phytase compared with the fungal phytase. These data suggest that a substantial part of the amino acid and energy responses observed following phytase supplementation in broiler chickens stems from reduced endogenous amino acid flows and that the capacity of different phytases to counteract the antinutritive properties of phytic acid vary.
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PMID:Influence of dietary phytic acid and source of microbial phytase on ileal endogenous amino acid flows in broiler chickens. 1893 Nov 80

A new phytase (APPA) with optimum pH 2.5--substantially lower than that of most of microbial phytases (pH 4.5-6.0)--was cloned from Yersinia frederiksenii and heterologously expressed in Escherichia coli. Containing the highly conserved motifs typical of histidine acid phosphatases, APPA has the highest identity (84%) to the Yersinia intermedia phytase (optimal pH 4.5), a member of histidine acid phosphatase family. Based on sequence alignment and molecular modeling of APPA and related phytases, APPA has only one divergent residue, Ser51, in close proximity to the catalytic site. To understand the acidic adaptation of APPA, five mutants (S51A, S51T, S51D, S51K, and S51I) were constructed by site-directed mutagenesis, expressed in E. coli, purified, and characterized. Mutants S51T and S51I exhibited a shift in the optimal pH from 2.5 to 4.5 and 5.0, respectively, confirming the role of Ser51 in defining the optimal pH. Thus, a previously unrecognized factor other than electrostatics--presumably the side-chain structure near the active site--contributes to the optimal pH for APPA activity. Compared with wild-type APPA, mutant S51T showed higher specific activity, greater activity over pH 2.0-5.5, and increased thermal and acid stability. These properties make S51T a better candidate than the wild-type APPA for use in animal feed.
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PMID:Improvement of Yersinia frederiksenii phytase performance by a single amino acid substitution. 1937 62

A 43-yr-old male presented with a 6-month history of episodes of coughing, shortness of breath and fever. He suffered from dyspnoea on minor exertion. The patient worked in a cattle feed factory and noticed that he had more complaints after his working hours. His symptoms could be ascribed to hypersensitivity pneumonitis due to contact with phytase, an enzyme added to cattle feed to strengthen bone and diminish phosphorus excretion. The diagnosis was supported by bibasal lung crackles on physical examination, restrictive ventilatory defect (with decreased diffusion capacity for carbon monoxide), typical radiographical findings, lymphocytosis in bronchoalveolar lavage fluid and a positive exposure test performed at the workplace. Blood examination showed high immunoglobulin G levels to phytase. After treatment and cessation of phytase contact the patient became symptom free and lung function normalised. Phytase should be considered as a cause of occupational hypersensitivity pneumonitis in the animal feed industry.
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PMID:Hypersensitivity pneumonitis caused by occupational exposure to phytase. 1948 53

The effect of phytase on nutrient digestibility in finishing pigs fed barley-based diet with soybean meal or canola meal as protein source was investigated. Six ileal-cannulated barrows (70 kg initial BW) were fed five diets in a 5 x 5 Latin square design with one added column. The five diets were based on barley-soybean meal (BSBM) or barley-canola meal (BCM) without or with phytase at 500 FTU/kg, and a casein-cornstarch-based diet, which was used to estimate standardised ileal AA digestibilities. No interactions were detected between phytase and diet on any of the response criteria measured except for apparent total tract N digestibility, which was reduced in BSBM diet but not BCM diet by phytase. Phytase increased (p < 0.01) apparent ileal and total tract P digestibility in both BSBM and BCM diets by at least 17 percentage units, and tended (p < 0.10) to increase the apparent ileal digestibilities of histidine, isoleucine, threonine, valine, cysteine, glycine and tyrosine. In conclusion, the effect of phytase in barley-based diets for finishing pigs on all response criteria measured in this study, except apparent total tract N digestibility, was not influenced by protein source.
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PMID:Nutrient digestibility in finishing pigs fed phytase-supplemented barley-based diets containing soybean meal or canola meal as a protein source. 1948 56

Four experiments were conducted to determine the nutritional value of flaxseed meal [FSM; 133 g of ether extract (EE) and 343 g of CP/kg of DM] for swine. In Exp. 1, apparent fecal digestibility (AD) of DM and EE, and the DE and NE contents were determined in growing pigs (n = 32; initial BW, 70 +/- 3 kg) and gestating sows (n = 24; parities, 2 to 4). Diets contained 0, 100, 200, or 300 g of FSM/kg at the expense of wheat, barley, and soybean meal. Fecal samples were collected for 3 d after a 9-d adaptation. The AD for DM and EE were 72.0 +/- 0.4% and 67.4 +/- 4.7%, respectively, for growing pigs and 68.0 +/- 0.5% and 48.9 +/- 1.9% for sows. The DE content was 3.51 and 3.54 Mcal/kg for growing pigs and gestating sows, and NE was estimated to be 2.43 and 2.44 Mcal/kg for growing pigs and sows, respectively. Five ileally cannulated barrows (initial BW, 38 +/- 3 kg) were fed semi-synthetic diets containing 400 g of FSM/kg for a 7-d period (4-d adaptation and 3-d collection) then 7 d of N-free diet to determine basal endogenous N losses in Exp. 2. Standardized ileal digestible AA contents were 29.6 +/- 1.0, 5.7 +/- 0.3, 12.1 +/- 0.8, 16.8 +/- 1.0, 10.3 +/- 0.4, 5.3 +/- 0.3, 14.0 +/- 0.7, 9.4 +/- 0.5, 2.9 +/- 0.2, and 13.8 +/- 0.8 g/kg of dry FSM for Arg, His, Ile, Leu, Lys, Met, Phe, Thr, Trp, and Val, respectively. In Exp. 3, the AD of P and the effects of phytase inclusion on P availability were determined. Five groups of 8 barrows (initial BW, 45 +/- 4 kg) were fed a 300 g of FSM/kg semi-synthetic diet with increasing concentrations of exogenous phytase [0, 575, 1,185, 2,400 and 2,570 phytase units (FTU)/kg]. The AD of P increased from 21 to 61% (P < 0.001). Broken-line analysis estimated the optimal phytase inclusion rate to be 1,415 FTU/kg of diet. Growth performance and carcass fatty acid (FA) profiles of pigs fed FSM were determined in Exp. 4. Two hundred pigs (100 barrows and 100 gilts; initial BW, 32 +/- 4 kg), blocked by sex, were housed in groups of 5 pigs per pen and fed 1 of 4 diets containing 0, 50, 100, or 150 g of FSM/kg. Six market pigs per diet were selected for carcass FA analysis. The ADG, ADFI, and G:F were not affected by dietary FSM (P > 0.05). Increasing FSM in the diet from 0 to 150 g of FSM/kg increased the alpha-linolenic acid content from 11.1 +/- 0.2 to 47.4 +/- 1.2 mg/g of backfat (P < 0.001) and from 5.0 +/- 0.1 to 10.1 +/- 0.6 mg/g of loin tissue (P < 0.001). Flaxseed meal despite its deficiency in lysine can be included up to 150 g/kg of diets for swine and will contribute to the enrichment of the carcass with n-3 fatty acids.
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PMID:Nutritional value of flaxseed meal for swine and its effects on the fatty acid profile of the carcass. 1961 10

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 cold storage. The full-length 2.5-kb fragment included an open reading frame of 1,302 bp and encoded a putative phytase of 45.3 kDa with a 50% amino acid identity to the Klebsiella pneumoniae phytase. The phytase contained the active site RHGXRXP and HD sequence motifs that are typical of histidine acid phosphatases. The enzyme was expressed in Escherichia coli, purified, and displayed the following characteristics: a high catalytic activity at low temperatures (retaining over 24% activity at 5 degrees C) and remarkably thermal lability (losing >96% activity after incubation at 60 degrees C for 2 min). The optimal phytase activity occurred at pH 5.5 and approximately 40 degrees C, and the enzyme activity rapidly decreased above 40 degrees C. When compared with mesophilic counterparts, the phytase not only exhibited a high activity at a low temperature, but also had a low K(m) and high k(cat). These temperature characteristics and kinetic parameters are consistent with low-temperature-active enzymes. To our knowledge, this would appear to be the first report of a low-temperature-active phytase and its heterogeneous expression.
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PMID:Novel low-temperature-active phytase from Erwinia carotovora var.carotovota ACCC 10276. 1988 63


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