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)

A periplasmatic phytase from a bacterium isolated from Malaysian waste water was purified about 173-fold to apparent homogeneity with a recovery of 10% referred to the phytase activity in the crude extract. It behaved as a monomeric protein with a molecular mass of about 42 kDa. The purified enzyme exhibited a single pH optimum at 4.5. Optimum temperature for the degradation of phytate was 65 degrees C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be KM=0.15 mmol/l and kcat=1164 s(-1) at pH 4.5 and 37 degrees C. The purified enzyme was shown to be highly specific. Among the phosphorylated compounds tested, phytate was the only one which was significantly hydrolysed. Some properties such as considerable activity below pH 3.0, thermal stability and resistance to pepsin make the enzyme attractive for an application as a feed supplement.
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PMID:Purification and characterization of a bacterial phytase whose properties make it exceptionally useful as a feed supplement. 1751 Jul 80

The effects of phytic acid and microbial phytase on the flow and composition of endogenous protein at the terminal ileum of broiler chickens were investigated using the peptide alimentation method. Phytic acid (fed as the sodium salt) was included in a synthetic diet at 8.5, 11.5 and 14.5 g/kg (or 2.4, 3.2 and 4.0 g/kg phytate-phosphorus) and each diet was fed without or with an Escherichia coli-derived microbial phytase at 500 phytase units/kg diet. A control containing no phytate was fed as a comparison to estimate basal endogenous flows. Ingestion of phytic acid increased (P < 0.05) the flow of endogenous amino acids and N by an average of 47 % at the lowest phytic acid concentration and 87 % at the highest. The addition of microbial phytase reduced (P < 0.05) the inimical effects of phytic acid on endogenous amino acid flow at all dietary phytic acid levels. The composition of endogenous protein was also influenced (P < 0.10-0.001) by increasing phytic acid concentrations and phytase addition. The effects of phytic acid and phytase on endogenous flow and composition of endogenous protein, however, varied depending on the amino acid. It is concluded that the effects of phytase on amino acid digestibility may be mediated, in part, through a route of reduced endogenous loss.
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PMID:Effect of phytic acid and microbial phytase on the flow and amino acid composition of endogenous protein at the terminal ileum of growing broiler chickens. 1752 77

A novel thermostable phytase gene was cloned from Aspergillus fumigatus WY-2. It was 1459 bp in size and encoded a polypeptide of 465 amino acids. The gene was expressed in Pichia pastoris GS115 as an extracellular enzyme. The expressed enzyme was purified to homogeneity and biochemically characterized. The purified enzyme had a specific activity of 51 U/mg with an approximate molecular mass of 88 kDa. The optimum pH and temperature for activity were pH 5.5 and 55 degrees C, respectively. After incubation at 90 degrees C for 15 min, it still remained at 43.7% of the initial activity. The enzyme showed higher affinity for sodium phytate than other phosphate conjugates, and the K(m) and K(cat) for sodium phytate were 114 microM: and 102 s(-1), respectively. Incubated with pepsin at 37 degrees C for 2 h at the ratio (pepsin/phytase, wt/wt) of 0.1, it still retained 90.1% residual activity. These exceptional properties give the newly cloned enzyme good potential in animal feed applications.
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PMID:Cloning, expression, and enzyme characterization of an acid heat-stable phytase from Aspergillus fumigatus WY-2. 1753 60

The interactions of sodium dodecyl sulfate (SDS) and two glyco-variants of the enzyme phytase from Peniophora lycii were investigated. One variant (Phy) was heavily glycosylated while the other (dgPhy) was enzymatically deglycosylated. Effects at 24 degrees C of titrating SDS to Phy and dgPhy were studied by Isothermal Titration Calorimetry (ITC) and Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. Comparisons of results for the two variants were used to elucidate glycan-surfactant interrelationships. The CD spectra suggested that both the native and the SDS-denatured states of the two variants were mutually similar, and hence that the denaturation process was structurally equivalent for the two glyco-variants. The denatured state was far from fully unfolded and probably retained a substantial content of native-like structure. Furthermore, it was found that the glycans brought about only a small increase in the resistance towards SDS induced denaturation. The SDS concentration required to denature half of the protein molecules differed less than 1 mM for the two variants. The affinity for SDS of both variants was unusually low. The amount of bound SDS (w/w) at different stages of the binding isotherm was 3-10 times lower than that reported for the most previously investigated globular proteins. Analysis of the relative affinity of the glycan and peptide moieties suggested that the carbohydrates bind much less surfactant. At saturation, glycans adsorbed about half as much SDS (in g/g) as the peptide moiety of Phy and about five times less than average proteins.
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PMID:Glycoprotein-surfactant interactions: a calorimetric and spectroscopic investigation of the phytase-SDS system. 1761 35

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 frame that consisted of 1311 bp encoding a 436-amino-acid protein, which had a deduced molecular mass of 46.3 kDa. The phytase appA belongs to the histidine acid phosphatase family and exhibits the highest identity (70.1%) with C. braakii phytase. The gene was overexpressed in P. pastoris. The secretion yield of recombinant appA protein was accumulated to approximately 4.2 mg.mL(-1), and the enzyme activity level reached 15,000 U x mL(-1), which is higher than any previous reports. r-appA was glycosylated, as shown by Endo H treatment. r-appA was purified and characterized. The specific activity of r-appA for sodium phytate was 3548 U.mg(-1). The optimum pH and temperature for enzyme activity were 4.5 and 55 degrees C, respectively. r-appA was highly resistant to pepsin or trypsin treatment. This enzyme could be an economic and efficient alternative to the phytases currently used in the feed industry.
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PMID:A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris. 1765 39

Ten different strains of Thermomyces lanuginosus, isolated from composting soils were found to produce phytase when grown on PSM medium. The wild type strain CM was found to produce maximum amount ofphytase (4.33 units/g DW substrate). Culturing T. lanuginosus strain CM on medium containing wheat bran and optimizing other culture conditions (carbon source, media type, nitrogen source, level of nitrogen, temperature, pH, inoculum age, inoculum level and moisture), increased the phytase yield to 13.26 units/g substrate. This culture was further subjected to UV mutagenesis for developing phytase hyperproducing mutants. The mutant (TL-7) showed 2.29-fold increase in phytase activity as compared to the parental strain. Employing Box-Behnken factor factorial design of response surface methodology resulted in optimized phytase production (32.19 units/g of substrate) by mutant TL-7. A simple two-step purification (40.75-folds) ofphytase from mutant TL-7 was achieved by anion exchange and gel filtration chromatography. The purified phytase (approximately 54 kDa) was characterized to be optimally active at pH 5.0 and temperature 70 degrees C, though the enzyme showed approximately 70% activity over a wide pH and temperature range (2.0-10.0 and 30-90 degrees C, respectively). The phytase showed broad substrate specificity with activity against sodium phytate, ADP and riboflavin phosphate. The phytase from T. lanuginosus was thermoacidstable as it showed up to 70% residual activity after exposure to 70 degrees C at pH 3.0 for 120 min. The enzyme showed Km 4.55 microM and Vmax 0.833 microM/min/mg against sodium phytate as substrate.
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PMID:Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7. 1789 92

The extracellular phytase in the supernatant of cell culture of the marine yeast Kodamaea ohmeri BG3 was purified to homogeneity with a 7.2-fold increase in specific phytase activity as compared to that in the supernatant by ammonium sulfate fractionation, gel filtration chromatography (Sephadextrade mark G-75), and anion-exchange chromatography (DEAE Sepharose Fast Flow Anion-Exchange). According to the data from sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular mass of the purified enzyme was estimated to be 98.2 kDa while the molecular mass of the purified enzyme was estimated to be 92.9 kDa and the enzyme was shown to be a monomer according to the results of gel filtration chromatography. The optimal pH and temperature of the purified enzyme were 5.0 and 65 degrees C, respectively. The enzyme was stimulated by Mn(2+), Ca(2+), K(+), Li(+), Na(+), Ba(2+), Mg(2+) and Co(2+) (at a concentrations of 5.0 mM), but it was inhibited by Cu(2+), Hg(2+), Fe(2+), Fe(3+), Ag(+), and Zn(2+) (at a concentration of 5.0 mM). The enzyme was also inhibited by phenylmethylsulfonyl fluoride (PMSF), iodoacetic acid (at a concentration of 1.0 mM), and phenylgloxal hydrate (at a concentration of 5.0 mM), and not inhibited by EDTA and 1,10-phenanthroline (at concentrations of 1.0 mM and 5.0 mM). The K (m), V (max), and K (cat) values of the purified enzyme for phytate were 1.45 mM, 0.083 micromol/ml . min, and 0.93 s(-1), respectively.
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PMID:Purification and characterization of extracellular phytase from a marine yeast Kodamaea ohmeri BG3. 1804 Jul 41

A protocol to assess the potential release of dissolved reactive phosphorus (DRP) by enzymatic hydrolysis of dissolved organic phosphorus (DOP) in waters (sediment porewater and sewage liquors in this study) under environmental conditions is presented. This protocol enables the quantification of different classes of DOP compounds using a variety of phosphatase enzymes, i.e., alkaline phosphatase, phosphodiesterase, and phytase. All experiments were carried out within the pH range of most natural waters, i.e., at neutral (pH 7) or slightly alkaline pH (pH 9). Tri-sodium citrate and sodium dodecyl sulfate (SDS) were used in the assays to prevent interferences due to adsorption processes in the presence of multivalent metallic cations and to minimize protein binding. Applying this protocol revealed that labile phosphate monoesters always represented the largest fraction of enzymatically hydrolyzed P in sewage liquors and sediment porewater. Total enzymatically hydrolyzable P (EHP) represented only 16% of the TDP in the sediment porewater but up to 43% in sewage liquors. Because most of the enzymes used in this study are likely to exist in aquatic ecosystems, the EHP fraction might represent a source of potentially bioavailable P of similar magnitude to DRP.
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PMID:A protocol to assess the enzymatic release of dissolved organic phosphorus species in waters under environmentally relevant conditions. 1804 29

Debaryomyces castellii phytase was purified to homogeneity in a single step by hydrophobic interaction chromatography. Its molecular mass is 74 kDa with 28.8% glycosylation. Its activity was optimal at 60 degrees C and pH 4.0. The K (m) value for sodium phytate was 0.532 mM. The enzyme exhibited a low specificity and hydrolyzed many phosphate esters. The phytase fully hydrolyzed myo-inositol hexakisphosphate (or phytic acid, Ins P(6)) to inositol and inorganic phosphate. The sequence of Ins P(6) hydrolysis was determined by combining results from high-performance ionic chromatography and nuclear magnetic resonance. D. castellii phytase is a 3-phytase that sequentially releases phosphate groups through Ins (1,2,4,5,6) P(5), Ins (1,2,5,6) P(4), Ins (1,2,6) P(3), Ins (1,2) P(2), Ins (1 or 2) P(1), and inositol (notation 3/4/5/6/1 or 2).
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PMID:Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923. 1804 51

The possible interaction between dietary electrolyte balance (DEB=Na+K-Cl, mEq/kg of diet) and microbial phytase on the performance and nutrient utilization of broiler starters and litter quality was examined in this study. A 4 x 2 factorial arrangement of treatments was used with 4 levels of DEB (150, 225, 300, and 375 mEq/kg of diet) and 2 levels of phytase (0 and 500 phytase units/kg of diet). Experimental diets were based on corn, soybean meal, and canola meal and were formulated to contain a nonphytate P level of 3 g/kg. The DEB levels were altered by the use of sodium bicarbonate and ammonium chloride. Each diet was offered to 6 replicates of 8 birds each from d 1 to 21. Increasing the DEB values from 150 to 300 mEq/kg had no effect (P>0.05) on the weight gains and feed per gain, but the gains were lowered (P<0.05) and the feed per gain was increased (P<0.05) at 375 mEq/kg. Feed intake was unaffected (P>0.05) by DEB levels. Supplemental phytase improved (P<0.05) the weight gains and feed intake at all DEB levels. Feed per gain was lowered (P<0.05) by phytase addition, but a tendency for a DEB x phytate interaction (P=0.06) was also observed, indicating that the responses to phytase may be affected by DEB level. The responses in feed per gain were greater at the lowest DEB level, and phytase addition had no effect on feed per gain at the highest DEB level. Dietary electrolyte balance levels had no effect on the AME(n) and ileal N digestibility to 300 mEq/kg, but lowered (P<0.05) both criteria at 375 mEq/kg. Phytase addition improved (P<0.05) the AME(n) and ileal N digestibility. The improvements in AME(n) with 500 U/kg of phytase addition in 150, 225, and 275 mEq/kg DEB were 53, 60, and 38 kcal/kg of DM, respectively. The main effect of DEB was significant (P<0.05) only for the ileal availability of Na and Cl, whereas added phytase influenced (P<0.05) the ileal availability of Ca, P, Na, K, and Cl. The effects of DEB were significant (P<0.05) for apparent ileal digestibility of all amino acids, except Ala (P=0.09), Arg, Met, and cystine. In general, the digestibilities of amino acids were unaffected when the DEB level was increased from 150 to 225 mEq/kg of diet, but decreased at the 300 and 375 mEq/kg levels. Phytase addition improved (P<0.06 to 0.05) ileal digestibility of all amino acids, except Met and Tyr. Increasing DEB had adverse effects on excreta scores and DM content. Phytase addition, however, had no effect on excreta quality. The overall results of the present study suggest that variability in phytase responses in nutrient utilization may be explained, in part, by differences in dietary electrolyte levels.
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PMID:Influence of dietary electrolyte balance and microbial phytase on growth performance, nutrient utilization, and excreta quality of broiler chickens. 1833 88


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