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)

Three experiments were conducted to determine the effects of phytase, excess Zn, or their combination in diets for nursery pigs. In all experiments, treatments were replicated with five to seven pens of six to seven pigs per pen, dietary Ca and available P (aP) levels were decreased by 0.1% when phytase was added to the diets, excess Zn was added as ZnO, a basal level of 127 mg/kg of Zn (Zn sulfate) was present in all diets, and the experimental periods were 19 to 21 d. In Exp. 1, pigs (5.7 kg and 18 d of age) were fed two levels of phytase (0 or 500 phytase units/kg) and three levels of excess Zn (0, 1,000, or 2,000 ppm) in a 2 x 3 factorial arrangement. Added Zn linearly increased ADG and ADFI during Phase 1 (P = 0.01 to 0.06), Phase 2 (P = 0.02 to 0.09), and overall (P = 0.01 to 0.02). Gain:feed was linearly increased by Zn during Phase 1 (P = 0.01) but not at other times. Dietary phytase decreased ADG in pigs fed 1,000 or 2,000 ppm Zn during Phase 2 (Zn linear x phytase interaction; P = 0.10), did not affect (P = 0.27 to 0.62) ADFI during any period, and decreased G:F during Phase 2 (P = 0.01) and for the overall (P = 0.07) period. Plasma Zn was increased by supplemental Zn (Zn quadratic, P = 0.01) but not affected (P = 0.70) by phytase addition. In Exp. 2, pigs (5.2 kg and 18 d of age) were fed two levels of phytase (0 or 500 phytase units/kg) and two levels of Zn (0 or 2,000 ppm) in a 2 x 2 factorial arrangement. Supplemental Zn increased ADG and G:F during Phase 2 (P = 0.02 to 0.09) and overall (P = 0.07 to 0.08), but it had no effect (P = 0.11 to 0.89) on ADG during Phase 1 or ADFI during any period. Phytase supplementation increased ADG (P = 0.06) and G:F (P = 0.01) during Phase 2. Gain:feed was greatest for pigs fed 2,000 ppm Zn and phytase (Zn x phytase interaction; P = 0.01). Bone (d 20) and plasma Zn (d 7 and 20) were increased (P = 0.01) by added Zn but not affected (P = 0.51 to 0.90) by phytase. In Exp. 3, pigs (5.7 kg and 19 d of age) were fed a basal diet or the basal diet with Ca and aP levels decreased by 0.10% and these two diets with or without 500 phytase units/kg. Supplemental phytase had no effect (P = 0.21 to 0.81) on growth performance. Reduction of dietary Ca and aP decreased (P = 0.02 to 0.08) ADG, ADFI, and G:F for the overall data. These results indicate that excess dietary supplemental Zn increases ADG and plasma and bone Zn concentrations. Dietary phytase did not affect plasma or bone Zn concentrations.
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PMID:Effects of supplemental dietary phytase and pharmacological concentrations of zinc on growth performance and tissue zinc concentrations of weanling pigs. 1564 11

Phytases catalyze the hydrolysis of phytic acid (myo-inositol hexakisphosphate), the most abundant inositol phosphate in cells. Phytases are of great commercial importance because their use as food and animal feed supplement has been approved by many countries to alleviate environmental and nutritional problems. Although acid phytases have been extensively studied, information regarding alkaline phytases is limited. Alkaline phytases with unique catalytic properties have been identified in plants, however, there is no report on the purification or structural properties. In this paper, we describe the purification of alkaline phytase from plant tissue. The purification was challenging because of contamination from non-specific phosphatases and acid phytases and low endogenous concentration. The purification of alkaline phytase from pollen grains of Lilium longiflorum involved selective precipitation by heat and ammonium sulfate followed by anion exchange and chromatofocusing chromatography and, finally, gel electrophoresis. Alkaline phytase was purified approximately 3000-fold with an overall recovery of 4.2%. The native molecular mass was estimated to be in the range of 118+/-7 kDa by Ferguson plot analysis and Mr of denatured protein in the range of 52-55 kDa by SDS-PAGE suggesting that the enzyme is a homodimer. Separation by 2-D gel and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric analysis of separated proteins indicates the presence of multiple mass and charge isoforms with pI values between 7.3 and 8.3. To our knowledge, this is the first alkaline phytase to be purified from plant sources. The unique properties suggest that the enzyme has the potential to be useful as a feed and food supplement.
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PMID:Alkaline phytase from Lilium longiflorum: purification and structural characterization. 1619 25

Five copper (Cu) sources were studied at pH 2.5, 5.5, and 6.5 to determine how Cu affects phytate phosphorus (PP) hydrolysis by phytase at concentrations up to 500 mg/kg diet (60 min, 40-41 degrees C). Subsequently, Cu solubility with and without sodium phytate was measured. Adding Cu inhibited PP hydrolysis at pH 5.5 and pH 6.5 (P < 0.05). This inhibition was greater with higher concentrations of Cu. Tri-basic copper chloride and copper lysinate inhibited PP hydrolysis much less than copper sulfate pentahydrate, copper chloride, and copper citrate (P < 0.05). A strong negative relationship was observed between PP hydrolysis and soluble Cu at pH 5.5 (r = -0.76, P < 0.0001) and 6.5 (r = -0.54, P < 0.0001). In conclusion, pH, Cu concentration, and source influenced PP hydrolysis by phytase in vitro and were related to the amount of soluble Cu and the formation of insoluble copper-phytin complexes.
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PMID:Effects of copper source and concentration on in vitro phytate phosphorus hydrolysis by phytase. 1650 35

Phytase (myo-inositol-1,2,3,4,5,6-hexakisphosphate phosphohydrolase, EC 3.1.3.26) catalyses the stepwise hydrolysis of phytic acid (myo-inositol hexakisphosphate). Phytases are of great commercial importance due to their usage as supplement of food and animal feed, which can cater to nutrition demands and alleviate environmental problems, has been approved by many countries. Although acid phytases have been extensively studied, information regarding the phytases from Citrobacter is limited. In the work presented, a phytase was separated from Citrobacter freundii. After steps of electrophoretic homogeneity by successive ammonium sulfate between 60% and 80% saturation precipitation, DEAE-Sepharose ion-exchange chromatography and gel filtration through Superdex HR 10/30, final gel elution resulted in a 41.3-fold purification and yield of 9.3%. Gel elution is an effective method to purify the protein which contaminated with a few other proteins. The purified preparations were used in subsequent characterization studies. Based on SDS-PAGE analysis, the molecular weight of the purified phytase was calculated to be approximately 45.0kDa in monomeric form. The pure enzyme has an optimum pH of 4.0 to approximately 4.5. It was found stable between pH5.0 to approximately 7.0, about 90% of the enzyme activity was retained at 37 degrees C for 60min. The phytase has an optimum temperature of 40 degrees C which was lower than that of other phytases from Aspergillus or E. coli (average 50 to approximately 60 degrees C) and was close to the temperature of gastrointestinal tract in animals (37 to approximately 40 degrees C). Thus the enzyme is a promising candidate for animal feed applications. Activity of the purified phytase was influenced by changing the reaction temperature. Data showed that the enzyme retained its activity over a long period when stored at 4 degrees C, whereas thermal inactivation studies indicated that the enzyme lost 100% activity after treatment at 60 degrees C for 4min. The Km values of the phytase for dodecasodium phytate at 37 degrees C was 0.85nmol/L with a Vmax 0.53IU/(mg x min). Phytase activity was strongly inhibited by SDS, Zn2+ and moderately inhibited by Cu2+, Cr3+, Fe2+ and Fe3+. Activity was not significantly affected by EDTA, K+, Mg2+ and Ca2+. The phytase has excellent resistance to trypsin, but not pepsin. The N-terminal amino acids sequence of the phytase protein was determined as QCAPEGYQLQQVLMM which exhibited about 80% homology to Glucose-1-phosphatases from E. coli, Shigella flexneri and Salmonella, whereas it did not show apparent sequence similarity with any other phytase listed in the databases. Initial characterization of the purified enzyme suggested that it is a potential candidate for use as an animal feed supplement.
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PMID:[Purification and properties of Citrobacter freundii phytase]. 1657 82

The phytase production by Sporotrichum thermophile TLR50 was recorded on all the commonly used animal feed ingredients tested to varying degrees in solid-state fermentation. Enzyme production increased to 180 U/g of dry moldy residue (DMR) in sesame oil cake at 120 h and 45 degrees C at the initial substrate-to-moisture ratio of 1:2.5 and aw of 0.95. Supplementation of sesame oil cake with glucose and ammonium sulfate further enhanced phytase titer (282 U/g of DMR). An overall 76% enhancement in phytase production was achieved owing to optimization. The mold secreted acid phosphatase, amylase, xylanase, and lipase along with phytase. By the action of phytase, inorganic phosphate was liberated efficiently, leading to dephytinization of sesame oil cake.
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PMID:Phytase production by thermophilic mold Sporotrichum thermophile in solid-state fermentation and its application in dephytinization of sesame oil cake. 1672 Sep 4

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

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

Statistical experimental designs were applied for the optimization of phytase production by a marine yeast Kodamaea ohmeri BG3 in a cost-effective oats medium. Using Plackett-Burman design, oats, ammonium sulfate and initial pH were identified as significant factors and these factors were subsequently optimized using a central composite design (CCD). The optimum variables that supported maximum enzyme activity were oats 1.0%, ammonium sulfate 2.3%, glucose 2.0%, NaCl 2.0% and initial pH 6.3. The validity of the optimized variables was verified in shake-flasks level. An overall 9-fold enhancement in phytase activity (62.0-->575.5 U/ml) was attained due to the optimization.
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PMID:Production of phytase by a marine yeast Kodamaea ohmeri BG3 in an oats medium: optimization by response surface methodology. 1818 Jan 56

The marine yeast strain Kodamea ohmeri BG3 isolated from the gut of a marine fish (Hexagrammes otakii) was found to secrete a large amount of phytase into the medium. The crude phytase produced by this marine yeast showed the highest activity at pH 5.0 and 65 degrees C. The optimal medium for phytase production contained oat 10.0 g/l, ammonium sulfate 15.0 g/l, glucose 30 g/l, and NaCl 20.0 g/l, while the optimal cultivation conditions for phytase production were pH 5.0, a temperature of 28 degrees C, and a shaking speed of 170 rpm. Under the optimal conditions, over 557.9 mU/ml of phytase activity was produced within 72 h of fermentation at the shake flask level. This is a very high level of phytase activity produced by yeasts. We think that the medium and process for phytase production by the marine yeast strain were very simple, and such marine yeast from the gut of natural marine fish may have a potential application in the maricultural industry and marine environmental protection. The results demonstrate that phytate was actively degraded by the crude phytase within a short period.
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PMID:Phytase production by a marine yeast Kodamea ohmeri BG3. 1840 48


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