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)

The phytase of Sporotrichum thermophile was purified to homogeneity using acetone precipitation followed by ion-exchange and gel-filtration column chromatography. The purified phytase is a homopentamer with a molecular mass of approximately 456kDa and pI of 4.9. It is a glycoprotein with about 14% carbohydrate, and optimally active at pH 5.0 and 60 degrees C with a T(1/2) of 16h at 60 degrees C and 1.5h at 80 degrees C. The activation energy of the enzyme reaction is 48.6KJmol(-1) with a temperature quotient of 1.66, and it displayed broad substrate specificity. Mg(2+) exhibited a slight stimulatory effect on the enzyme activity, while it was markedly inhibited by 2,3-butanedione suggesting a possible role of arginine in its catalysis. The chaotropic agents such as guanidinium hydrochloride, urea and potassium iodide strongly inhibited phytase activity. Inorganic phosphate inhibited enzyme activity beyond 3mM. The maximum hydrolysis rate (V(max)) and apparent Michaelis-Menten constant (K(m)) for sodium phytate were 83nmolmg(-1)s(-1) and 0.156mM, respectively. The catalytic turnover number (K(cat)) and catalytic efficiency (K(cat)/K(m)) of phytase were 37.8s(-1) and 2.4x10(5)M(-1)s(-1), respectively. Based on the N-terminal and MALDI-LC-MS/MS identified amino acid sequences of the peptides, the enzyme did not show a significant homology with the known phytases.
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PMID:Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile. 1905 69

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, was cloned using degenerate PCR and thermal asymmetric interlaced PCR. To our knowledge, this is the first report of detection of phytase activity and cloning of phytase gene from Pedobacter. PhyP belongs to beta-propeller phytase family and shares very low identity ( approximately 28.5%) with Bacillus subtilis phytase. The purified recombinant enzyme (r-PhyP) from Escherichia coli displayed high specific activity for sodium phytate of 24.4 U mg(-1). The optimum pH was 7.0, and the optimum temperature was 45 degrees C. The K (m), V (max), and k (cat) values were 1.28 mM, 71.9 micromol min(-1) mg(-1), and 45.1 s(-1), respectively. Compared with Bacillus phytases, r-PhyP had higher relative activity at 25 degrees C (r-PhyP (>50%), B. subtilis phytase (<8%)) and hydrolyzed phytate from soybean with greater efficacy at neutral pH. These characteristics suggest that r-PhyP might be a good candidate for an aquatic feed additive in the aquaculture industry.
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PMID:A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive. 1913 77

This study was undertaken to screen and select potent phytate degrading lactic acid bacteria and to evaluate their additional characteristic features. Forty lactic acid bacterial strains were isolated from different sources and screened for their ability to degrade myo-inositol hexaphosphate or IP(6) by cobalt chloride staining (plate assay) method, using calcium or sodium salt of phytic acid as substrate. All the forty isolates were able to degrade calcium phytate. However, only two Pediococcus pentosaceus strains (CFR R38 and CFR R35) were found to degrade sodium phytate. These strains showed phytase activity of 213 and 89 U at 50 degrees C, respectively and poor acid phosphatase activity. These strains were further evaluated for additional characteristic features. At pH 2, P. pentosaceus strains CFR R38 and CFR R35 showed 50.7 and 48.5 percentage survivability after 2 h of incubation respectively and they could also withstand 0.3% ox-bile. These cultures exhibited 54.6 and 44.8% of hydrophobicity to xylene, antibacterial activity against food borne pathogens and possessed beta-galactosidase activity. The resistance pattern to several antibiotics was also analyzed. The present study indicates that these strains, having phytate degrading ability and other characteristic features can be exploited as starter cultures in fermented foods to improve the mineral bioavailability.
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PMID:Screening, selection and characterization of phytic acid degrading lactic acid bacteria from chicken intestine. 1948 Dec 82

A high phytase-producing strain of Aspergillus niger N-3 was identified by screening 104 microbial strains. The gene for A. niger N-3 was cloned and expressed in Pichia pastoris. The coding region without the introns and putative signal sequence was comprised of 1347 nucleotides. It encoded a polypeptide of 448 amino acids, exhibiting high amino acid sequence homologies (94.87%) with the typical phytase of A. niger NRRL 3135. The molecular mass of the recombinant phytase as determined by SDS-PAGE was 60-70 kDa, with maximum activity at approximately 55 degrees C (after incubation at 10 min). The phytase retained about 45% of its enzymatic activity under heat treatment at 90 degrees C for 5 min. It showed a greater affinity for sodium phytate than for p-nitrophenyl phosphate. Dual optima pH (2.0 and 5.5) was gained. The activity at pH 2.0 was about 30% higher than at pH 5.5, which was more suitable to the circumstance of the stomachs of monogastric animals. The extent of glycosylation influenced the characterization of phytase. The deglycosylated phytase showed pH optima at 3.5 and 5.5, and the molecular mass had dropped to 50 kDa.
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PMID:Identification, characterization, and overexpression of a phytase with potential industrial interest. 1948 88

Phosphohydrolysis of organic phosphorus compounds by acid phosphatases (EC 3.1.3.1 and EC 3.1.3.2) is an important method for efficient removal of phosphorus from high concentration organic wastewater. Another important method is supplementation of animal feed with phytase (EC 3.1.3.8 and EC 3.1.3.26), which improves the availability of phytate-phosphates (phosphate that are hydrolyzed by phytases), making it possible to add less phosphate to animal feed and resulting in the excretion of less phosphorus by the animals. In the present study, we purified a novel phytase from the wastewater treatment yeast Hansenula fabianii J640 (Hfphytase), cloned the 1456 bp open reading frame (ORF) encoding Hfphytase, and characterized Hfphytase. The molecular weight of Hfphytase after deglycosylation by PNGaseF was 49 kDa. The optimal pH and temperature for enzyme activity were 4.5 and 50 degrees C, respectively. Hfphytase exhibits 40% identity with Debaryomyces castellii phytase, 37% identity with Aspergillus niger PhyB, and 34% identity with Saccharomyces cerevisiae Pho5p. Recombinant Hfphytase was transformed and expressed in Pichia pastoris. The yield was 23 g/l by jar fermenter cultivation. The marked phosphohydrolysis activity exhibited by Hfphytase on six substrates (pNP-P, sodium phytate, glucose-1 phosphate, glucose-6 phosphate, alpha-glycerophosphate and beta-glycerophosphate) indicated that it is a non-specific acid phosphatase.
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PMID:Cloning and characterization of a novel phytase from wastewater treatment yeast Hansenula fabianii J640 and expression in Pichia pastoris. 1966 57

An optimized Citrobacter braakii phytase gene, appA-c, was chemically synthesized by oligonucleotides synthesis and over-lap PCR method. The appA-c gene encoding 423 amino acids was cloned into expression vector pPIC9 and transformed into methylotropic yeast Pichia pastoris. From about 2000 transformants, 400 transformants exhibiting phytase activity were obtained. One transformant showing the strongest phytase activity was selected for detailed analyses in 5 L bioreactor. Under control of the highly-inducible alcohol oxidase gene (AOX1) promoter, the transformant was able to secrete 3.85 mg/ml protein to the culture supernatant in about 110 h methanol induction, which comprises of 12,116 U ml(-1) phytase activity. Further characterization of the recombinant phytase was conducted. The optimal pH and temperature for this recombinant phytase was about 4.0 and 50 degrees C, respectively. Fe3+, Zn2+ and Cu2+ could significantly inhibit the recombinant phytase enzyme activity. The specific activity of this recombinant enzyme was 3147 U mg(-1). The K(m) and V(max) values for sodium phytate were determined to be 0.5 mM and 3085 U/mg, respectively. To our knowledge, this is the first report of a chemically synthesized C. braakii appA gene heterologous expression with the highest expression level and highest phytase activity achieved. The novel gene optimization and synthesis method can be applied to other related researches.
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PMID:A new method for gene synthesis and its high-level expression. 1973

Five experiments were conducted to investigate the ability of different phytase products to improve P digestibility in finishing pigs. A corn-soybean meal basal diet containing 0.50% Ca, 0.32% P, and 0.40% Cr(2)O(3) was used to calculate apparent P and GE digestibility. Pigs were individually penned and fed their respective diet for ad libitum intake for 12 d before fecal sampling on d 13 and 14 and blood collection on d 14 for plasma P determination. Experiments 1 through 4 used gilts with across-trial average initial and final BW of 84 and 97 kg, respectively. Pigs were fed Natuphos (Exp. 1), OptiPhos (Exp. 2), Phyzyme (Exp. 3), or RonozymeP (Exp. 4) at 0, 200, 400, 600, 800, or 1,000 phytase units (FTU)/kg (where 1 FTU is defined as the quantity of enzyme required to liberate 1 micromol of inorganic P per min, at pH 5.5, from an excess of 15 micromol/L of sodium phytate at 37 degrees C). Experiment 5 used barrows with initial and final BW of 98 and 111 kg, respectively, and were fed diets containing 0, 500, or 1,000 FTU/kg of Natuphos, OptiPhos, Phyzyme, or RonozymeP. Pigs fed Natuphos (Exp. 1) and OptiPhos (Exp. 2) exhibited a linear and quadratic (P < 0.01) improvement in P digestibility with increasing levels of dietary phytase, whereas pigs fed Phyzyme (Exp. 3) and RonozymeP (Exp. 4) exhibited a linear (P < 0.01) improvement in apparent P digestibility with increasing levels of dietary phytase. In Exp. 5, the improvement in apparent P digestibility with increasing levels of dietary phytase was linear (P < 0.01) for Natuphos, Phyzyme, and RonozymeP, but was linear and quadratic (P < 0.01) for OptiPhos. Based on regression analysis, inorganic P release at 500 FTU/kg was predicted to be 0.070, 0.099, 0.038, and 0.030% for Natuphos, OptiPhos, Phyzyme, and RonozymeP, respectively. These estimates are comparable with those of pigs in Exp. 5, for which the estimated inorganic P release at 500 FTU/kg was 0.102, 0.039, and 0.028% for OptiPhos, Phyzyme, and RonozymeP, respectively, but not for the 0.034% value determined for Natuphos. The effect of dietary phytase on GE digestibility was inconsistent with a linear (P < 0.01) improvement in GE digestibility noted for OptiPhos (Exp. 2 and 5) and RonozymeP (Exp. 4), but the quadratic (P < 0.01) improvement for Natuphos. There was no effect of dietary phytase on plasma inorganic P. The data presented show clear improvements in P digestibility, with the estimated level of inorganic P release being dependent on phytase source and level.
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PMID:Effect of phytase on apparent total tract digestibility of phosphorus in corn-soybean meal diets fed to finishing pigs. 1978 8

A mature phytase cDNA, encoding 441 amino acids, from Eupenicillium parvum (BCC17694) was cloned into a Pichia pastoris expression vector, pPICZ alpha A, and was successfully expressed as active extracellular glycosylated protein. The recombinant phytase contained the active site RHGXRXP and HD sequence motifs, a large alpha/beta domain and a small alpha-domain that are typical of histidine acid phosphatase. Glycosylation was found to be important for enzyme activity which is most active at 50 degrees C and pH 5.5. The recombinant phytase displayed broad substrate specificity toward p-nitrophenyl phosphate, sodium-, calcium-, and potassium-phytate. The enzyme lost its activity after incubating at 50 degrees C for 5 min and is 50% inhibited by 5mM Cu(2+). However, the enzyme exhibits broad pH stability from 2.5 to 8.0 and is resistant to pepsin. In vitro digestibility test suggested that BCC17694 phytase is at least as effective as another recombinant phytase (r-A170) which is comparable to Natuphos, a commercial phytase, in releasing phosphate from corn-based animal feed, suggesting that BCC17694 phytase is suitable for use as phytase supplement in the animal diet.
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PMID:Biochemical characterization and in vitro digestibility assay of Eupenicillium parvum (BCC17694) phytase expressed in Pichia pastoris. 1981 56

1. A precision feeding experiment was conducted with broiler chickens, which were previously fed on diets with or without phytase, to study the effects of previous exposure to dietary phytase supplementation on the excretions of endogenous energy, nitrogen, amino acids and minerals. 2. Female Ross 308 broiler chickens, which had previously received one of 4 experimental diets (low P maize/soy diets (control, D), D + 250 international units of phytase per kg diet (FTU), D + 500 FTU and D + 2500 FTU) were used in the study. All birds were starved and then given 50 ml of glucose solution at 44 d of age. The birds were allocated to individual metabolism cages in a randomised block design with 8 replicates of each of the 4 dietary treatments. 3. Chickens which had been previously fed on diets supplemented with phytase excreted 32% less energy and 28% less dry matter per kg metabolic body weight (W(075)) from endogenous sources, compared to birds fed the unsupplemented diet. 4. Birds previously given phytase supplemented diets excreted 60% less sodium than those given the control diet, but there was no effect on all other minerals investigated. There was no effect of diet on the excretion of endogenous N, sialic acid or amino acids. 5. The results showed that the effects of feeding chickens on diets with supplementary phytase may continue for a few days after the diets are withdrawn. This suggests that previous exposure to phytase may alter the nutritive value of follow-on diets, which may be a commercially important effect.
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PMID:Previous exposure to dietary phytase reduces the endogenous energy losses from precision-fed chickens. 1990 39

The objective of the present study was to investigate the effect of dietary phytate and microbial phytase on the lipase activity, lipid metabolism and mRNA expressions of fatty acid synthase (FASN) and leptin in broiler chickens. The study was conducted as a 2 x 3 factorial arrangement of treatments with phytate phosphorus at 0.20 and 0.40 % (added as the sodium phytate) and supplemental microbial phytase at 0, 500, or 1000 phytase units/kg. The results showed that phytase improved (P < 0.05) the growth performance and ileal digestibility of nutrients of broilers, but phytate had no effect (P>0.05) on these parameters, except the decrease (P < 0.01) in the digestibility of Ca. Phytate decreased (P < 0.05) the lipase activity, serum total cholesterol (T-CHO) and hepatic TAG, and elevated (P < 0.01) serum NEFA and HDL cholesterol. Phytase decreased (P < 0.05) serum NEFA, but increased (P < 0.01) serum T-CHO and hepatic TAG. Phytate and phytase also influenced (P < 0.01) the mRNA expressions of leptin in the liver. There were significant (P < 0.05) interactions of phytate and phytase on the concentrations of serum TAG and LDL cholesterol, hepatic NEFA and T-CHO, and the mRNA expressions of FASN. The results suggest that phytate and phytase can affect lipase activity and lipid metabolism of broiler chickens.
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PMID:Effect of dietary sodium phytate and microbial phytase on the lipase activity and lipid metabolism of broiler chickens. 2000 70


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