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 phytase (EC 3.1.3.8) was extracted from rat intestinal bacterium, Klebsiella Sp. No. PG.-2, and purified 50-fold by ammonium sulphate fractionation, ion-exchange chromatography and gel filtration. The enzyme is inducible in nature. The pH optimum was at 6.0 for all the inositol phosphates studied and this characterized the enzyme as an acid phosphohydrolase. Of a range of potential substrates tested, only p-nitrophenyl phosphate alongwith the inositol phosphates was hydrolyzed. It exhibits a Km of 2.0 mM; temperature optimum of 37 degrees C and energy of activation 9,120 cal/mole for all the inositol phosphates studied. The activity was inhibited by Ag2+, Hg2+, Cu2+, fluoride and high substrate concentration.
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PMID:Phytase from Klebsiella Sp. No. PG-2: purification and properties. 216 21

Purified Aspergillus ficuum phytase's partial primary structure and amino acid and sugar composition were elucidated. Determination of kinetic parameters of the enzyme at different pH values and temperatures indicated no significant alteration of the Km for phytate while the Kcat was affected. The enzyme was able to release more than 51% of the total available Pi from phytate in a 3.0 hr assay at 58 degrees C, but the Kcat dropped to 15% of the initial rate. Substrate selectivity studies revealed phytate to be the preferred substrate. The pH optima of phytase was 5.0, 4.0, and 3.0 for phytate, ATP, and polyphosphate, respectively. The enzyme had varied sensitivity towards cations. While Ca++ and Fe++ produced no effect on the catalytic rate of the enzyme, Cu+, Cu++, Zn++, and Fe were found to be inhibitory. Mn++ was observed to enhance enzyme activity by 33% at 50 microM. Known inhibitors of acid phosphatases e.g. L (+)-tartrate, phosphomycin, and sodium fluoride had no effect on enzyme activity.
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PMID:Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. 285 7

Bile Cu accumulation in Cu-depleted chicks fed Cu concentrations between .56 and 1.56 mg Cu/kg (0, .5, or 1 mg supplemental Cu/kg) was used to investigate the effect of microbial phytase at 600 U/kg and 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] at 10 micrograms/kg on Cu bioavailability from dehulled soybean meal (SBM) and cottonseed meal (CSM). The bioavailability of Cu (relative to CuSO4.5H2O, which was set at 100%) in SBM and CSM was 43 and 39%, respectively. Phytase addition (600 U/kg diet) decreased Cu bioavailability in SBM to 21%, but did not affect that in CSM (34%). Copper bioavailability in SBM was not affected by addition of 1,25-(OH)2D3 (10 micrograms/kg diet), but that in CSM was nearly doubled by 1,25-(OH)2D3 supplementation.
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PMID:Effect of microbial phytase and 1,25-dihydroxycholecalciferol on dietary copper utilization in chicks. 789 99

Three groups of individually housed albino rats (n = 6, initial average weight = 47 g) were fed diets based on egg white and cornstarch (basal diet 8 g Ca, 5.2 g P, 0.76 g Mg, 100 mg Zn, 100 mg Fe, 50 mg Mn, 7 mg Cu, and 5 mg Cd per kilogram diet) over a 4-week period. Group I (controls) was fed the basal diet free of phytic acid (PA) and microbial phytase. In groups II and III cornstarch was replaced by 0.5% PA from NaPA (molar PA/Zn ratio approximately 5). In group III, 2,000 U of microbial phytase from Aspergillus niger per kilogram diet was added. Live weight gain, zinc status (zinc in plasma, femur, liver, and testes; activity of the plasma alkaline phosphatase), and apparent absorption of zinc, iron, copper, and manganese remained unchanged by the different dietary treatments. The apparent phosphorus absorption was highest in the phytase group. PA decreased and microbial phytase improved the apparent absorption of calcium and magnesium. Liver cadmium concentration, total liver and kidney cadmium content, as well as fractional liver and kidney cadmium accumulation in rats fed the diet containing PA were significantly higher than those in the controls. Phytase supplementation lowered liver and kidney cadmium accumulation. Differences in calcium and magnesium bioavailability due to PA and microbial phytase may be one factor in the alteration of tissue cadmium accumulation.
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PMID:Effect of phytic acid and microbial phytase on Cd accumulation, Zn status, and apparent absorption of Ca, P, Mg, Fe, Zn, Cu, and Mn in growing rats. 867 72

The extracellular activity of Aspergillus niger phytase at the end of the growth phase was 132 nkat/mL in a laboratory bioreactor. The purified enzyme has molar mass approximately 100 kDa, pH optimum at 5.0, temperature optimum at 55 degrees C and high pH and temperature stability. The Km for dodecasodium phytate, calcium phytate and 4-nitrophenyl phosphate are 0.44, 0.45 and 1.38 mmol/L, respectively. The enzyme is noncompetively inhibited by inorganic monophosphate (Ki = 2.85 mmol/L) and by Cu2+, Zn2+, Hg2+, Sn2+, Cd2+ ions and strongly by F- ones; it is activated by Ca2+, Mg2+ and Mn2+ ions. The substrate specificity of phytase is broad with the highest affinity to calcium phytate.
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PMID:Characterization of phytase produced by Aspergillus niger. 944 82

Bacillus species producing a thermostable phytase was isolated from soil, boiled rice, and mezu (Korean traditinal koji). The activity of phytase increased markedly at the late stationary phase. An extracellular phytase from Bacillus sp. KHU-10 was purified to homogeneity by acetone precipitation and DEAE-Sepharose and phenyl-Sepharose column chromatographies. Its molecular weight was estimated to be 46 kDa on gel filtration and 44 kDa on SDS-polyacrylamide gel elctrophoresis. Its optimum pH and temperature for phytase activity were pH 6.5-8.5 and 40 degrees C without 10 mM CaCl2 and pH 6.0-9.5 and 60 degrees C with 10 mM CaCl2. About 50% of its original activity remained after incubation at 80 degrees C or 10 min in the presence of 10 mM CaCl2. The enzyme activity was fairly stable from pH 6.5 to 10.0. The enzyme had an isoelectric point of 6.8. As for substrate specificity, it was very specific for sodium phytate and showed no activity on other phosphate esters. The Km value for sodium phytate was 50 microM. Its activity was inhibited by EDTA and metal ions such as Ba2+, Cd2+, Co2+, Cr3+, Cu2+, Hg2+, and Mn2+ ions.
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PMID:Purification and properties of extracellular phytase from Bacillus sp. KHU-10. 1159 62

Extracellular phytase produced by Aspergillus niger ATCC 9142 was purified to homogeneity by employing an initial ultrafiltration step, followed by chromatography using ion exchange, gel filtration and chromatofocusing steps. The purified enzyme was an 84 kDa, monomeric protein. It possessed a temperature optimum of 65 degrees C, and a pH optimum of 5.0. Km and Vmax values of 100 microM and 7 nmol/s, respectively, were recorded and these values fall well within the range of those previously reported for microbial phytases. Substrate specificity studies indicated that, while the enzyme could hydrolyse a range of non-phytate-based phosphorylated substrates, its preferred substrate was phytate. Phytase activity was moderately stimulated in the presence of Mg2+, Mn2+, Cu2+, Cd2+, Hg2+, Zn2+ and F- ions. Activity was not significantly affected by Fe2- or Fe3- and was moderately inhibited by Ca2+. The enzyme displayed higher thermostability at 80 degrees C than did two commercial phytase products. Initial characterisation of the purified enzyme suggested that it could be a potential candidate for use as an animal feed supplement.
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PMID:Purification and characterization of extracellular phytase from Aspergillus niger ATCC 9142. 1265 85

Absorption of selenium and copper is much lower in ruminants than in nonruminants. The low absorption of these minerals in ruminants is due to modifications that occur in the rumen environment. Selenium bioavailability is reduced by high dietary sulfur and the presence of cyanogenetic glycosides in certain legumes. Feeding organic selenium from selenomethionine or selenized yeast results in much higher tissue and milk selenium concentrations than are obtained with selenite. High dietary molybdenum in combination with moderate to high dietary sulfur results in formation of thiomolybdates in the rumen. Thiomolybdates greatly reduce copper absorption, and certain thiomolybdate species can be absorbed and interfere systemically with copper metabolism. Independent of molybdenum, high dietary sulfur reduces copper absorption perhaps via formation of copper sulfide. High dietary iron also reduces copper bioavailability. Dietary factors that affect bioavailability of zinc in ruminants are not well defined. Phytate does not affect zinc absorption in ruminants because microbial phytase in the rumen degrades phytate. Manganese is very poorly absorbed in ruminants, and limited research suggests that high dietary calcium and phosphorus may reduce manganese absorption.
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PMID:Trace mineral bioavailability in ruminants. 1273 Apr 54

A phytase (EC 3.1.3.8) from Pseudomonas syringae MOK1 was purified to apparent homogeneity in two steps employing cation and an anion exchange chromatography. The molecular weight of the purified enzyme was estimated to be 45 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The optimal activity occurred at pH 5.5 and 40 degrees C. The Michaelis constant (Km) and maximum reaction rate (Vmax) for sodium phytate were 0.38 mM and 769 U/mg of protein, respectively. The enzyme was strongly inhibited by Cu2+, Cd2+, Mn2+, and ethylenediaminetetraacetic acid (EDTA). It showed a high substrate specificity for sodium phytate with little or no activity on other phosphate conjugates. The enzyme efficiently released orthophosphate from wheat bran and soybean meal.
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PMID:Purification and characterization of a phytase from Pseudomonas syringae MOK1. 1462 9

Copper is often added to broiler diets at prophylactic concentrations as an antimicrobial despite purported chelation with and reduced utilization of phytin phosphorus. Therefore, male chicks were fed 0, 62.5, 125, 250, or 375 ppm Cu from Cu sulfate in combination with 600 phytase units (FTU)/kg phytase from 9 to 22 d of age (6 cages/diet, 8 birds/cage). Nonphytate phosphorus (NPP) and Ca were formulated to 0.2 and 0.7% of the diet, respectively. Three additional control diets were formulated to contain 0.27, 0.34, and 0.40% NPP, each with 0.7% Ca. Birds fed increasing concentrations of Cu with 600 FTU phytase/kg had linear reductions in performance characteristics (P < or = 0.05). Birds fed increasing concentrations of Cu with 600 FTU phytase/kg had linear increases in toe ash percentage (P < or = 0.027), but tibia ash percentage was not affected (P > 0.05). Birds fed increasing Cu concentrations with 600 FTU phytase/kg had linear reductions in apparent P retention as a percentage of total P (P < or = 0.0005). Supplementation with increasing concentrations of Cu to a diet containing 600 FTU phytase/kg resulted in decreases in 21 d BW, BW gain, feed consumption, feed conversion, tibia and toe ash weights, and apparent P retention as a percentage of total P. In this experiment, Cu supplementation did not reduce the efficacy of phytase (i.e., improvement in apparent P retention with phytase supplementation) but did decrease apparent P retention, BW gain, feed consumption, feed conversion, and tibia ash and toe ash weights.
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PMID:The effects of copper on the efficacy of phytase, growth, and phosphorus retention in broiler chicks. 1533 8


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