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)

Evaluations of the nutritional effect of antibiotics have largely centered on effects related to the digestibility and utilization of protein and energy. The current study evaluated the potential effect of virginiamycin (VIR) on P digestibility in swine. A total of 70 barrows (mean initial BW = 51 to 64 kg) were used in 4 nutrient-balance experiments. A basal, corn-soybean meal diet that was not supplemented with any inorganic source of P was used in each experiment. In Exp. 1, two diets were tested: basal vs. basal plus 11 mg/kg of VIR. In Exp. 2, four diets were used with a 2 x 2 factorial arrangement of 0 and 11 mg/kg of VIR and 0 and 750 phytase (PHY) units/kg of diet (PU/kg). Experiments 3 and 4 were the same as Exp. 2, except PHY was reduced to 300 PU/kg. For all experiments, VIR improved P digestibility (32.71 to 37.72%, P < 0.001) and Ca digestibility (54.99 to 58.30%, P = 0.002). The addition of PHY improved both P and Ca digestibility (P < 0.001); 750 PU/kg increased P digestibility 27.3% (from 34.6 to 61.9%, P < 0.001), whereas 300 PU increased it 13.8% (from 33.4 to 47.2%, P < 0.001). In an experiment conducted to evaluate the long-term effects of VIR on gut microbial profile, pigs (24 gilts and 8 barrows; mean BW = 29.1 +/- 0.50 kg) were fed a simple corn-soybean meal diet for 16 wk with a 2 x 2 factorial arrangement of VIR (0 and 11 mg/kg) addition and 0.15% dicalcium phosphate deletion. The long-term feeding of VIR in both the control diet and the diet with a marginally reduced P level resulted in a change in ileal microbial profile. A positive numerical increment in the number of phytate-utilizing bacteria was observed in both the normal and P-deleted diets (log unit increments of 12.4 and 17.2% over the respective controls, P = 0.13) when VIR was added. The addition of VIR also tended to affect lactobacilli populations (main effect, P = 0.11; interaction, P = 0.02); VIR decreased lactobacilli in the normal-P diet but did not affect this bacterial population in the P-deleted diet. In conclusion, the antibiotic VIR improves both Ca and P digestibility in pigs. The increase in digestibility is not as great as that provided by PHY, but because the potential mechanism of action (altered microbial populations) differs from that of PHY (direct addition of an enzyme), there can be a degree of additivity in P digestibility improvement when both products are used.
J Anim Sci 2007 Sep
PMID:Virginiamycin improves phosphorus digestibility and utilization by growing-finishing pigs fed a phosphorus-deficient, corn-soybean meal diet. 1746 24

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.
Biophys Chem 2007 Sep
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.
Curr Microbiol 2007 Sep
PMID:A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris. 1765 39

Wheat phytase was purified to investigate the action of the enzyme toward its pure substrate (phytic acid - myo-inositol hexakisphosphate) and its naturally occurring substrate (phytate globoids). Phytate globoids were purified to homogeneity from wheat bran, and their nutritionally relevant parameters were quantified by ICP-MS. The main components of the globoids were phytic acid (40% w/w), protein (46% w/w), and several minerals, in particular, K > Mg > Ca > Fe (in concentration order). Investigation of enzyme kinetics revealed that K(m) and V(max) decreased by 29 and 37%, respectively, when pure phytic acid was replaced with phytate globoids as substrate. Time course degradation of phytic acid or phytate globoids using purified wheat phytase was followed by HPIC identification of inositol phosphates appearing and disappearing as products. In both cases, enzymatic degradation initiated at both the 3- and 6-positions of phytic acid and end products were inositol and phosphate.
J Agric Food Chem 2007 Sep 05
PMID:Quantitative analysis of phytate globoids isolated from wheat bran and characterization of their sequential dephosphorylation by wheat phytase. 1769 44

The effect of an exogenous phytase and cellulase-containing enzyme formulation on nutrient digestibility and excretion was evaluated in 24 Holstein cows. Cows were fed corn silage- and alfalfa silage-based diets with or without a cellulase-phytase blend for 31 d in a continuous random design. Treatment groups were balanced for parity, days in milk, and mature-equivalent projected milk yield. Diets contained 37% forage, 18.3% crude protein, 35.4% neutral detergent fiber, 18% acid detergent fiber, and 0.42% P (no supplemental P). Cows were fed once daily in Calan doors and milked 2 times daily. Body weight and milk yield were recorded at each milking. Milk samples were collected on d 28 to 31 at 8 consecutive milkings. On d 28 to 31, fecal grab samples were collected every 8 h, with sampling times advanced by 2 h each day. Feces samples were pooled by cow. Feed and feces samples were analyzed for acid detergent lignin (used as an internal marker) and for N, P, neutral detergent fiber, and acid detergent fiber. Days in milk were similar between treatments, and body weight and milk yield were unaffected by treatment. Cows fed the enzyme formulation had reduced fecal dry matter, neutral detergent fiber, and acid detergent fiber excretion and reduced fecal excretion of N and P. Apparent digestibility of dry matter, acid detergent fiber, neutral detergent fiber, and N tended to increase with the enzyme formulation. Addition of an exogenous phytase and cellulase enzyme formulation to diets for lactating cows reduced fecal nutrient excretion.
J Dairy Sci 2007 Sep
PMID:Manure nutrient excretion by lactating cows fed exogenous phytase and cellulase. 1769 56

The application of biotechnological products in the feed industry has undergone explosive growth in recent years, and phytase from microorganism accounts for one-third of the entire feed enzyme market. In this study, some differences in the composition of protein and denaturation temperature between two commercial phytases were determined by HPLC and differential scanning calorimetry, which were derived from the same origin of E. coli. At the same time, we found that it was advantageous for near-infrared reflectance spectroscopy (NIRS) to display the protein differences in the commercial phytase, which is most important for ensuring the traceability of biotechnological products in feed and food safety control. Furthermore, NIRS could track the changes in phytase during the spray-drying process and the change of enzyme activity during storage of phytase. Our experiments proved that the information from NIRS could describe well the individual characteristics of the commercial phytase, which indicated that near-infrared reflectance spectra could be exploited to use in the registration system of commercial phytase.
J Agric Food Chem 2007 Sep 19
PMID:Near-infrared reflectance spectroscopy-based methods for phytase registration in feed industry. 1771 90

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.
Bioresour Technol 2008 Sep
PMID:Production of phytase by a marine yeast Kodamaea ohmeri BG3 in an oats medium: optimization by response surface methodology. 1818 Jan 56

Two novel phytase genes belonging to the histidine acid phosphatase family were cloned from Yersinia rohdei and Y. pestis and expressed in Pichia pastoris. Both the recombinant phytases had high activity at pH 1.5-6.0 (optimum pH 4.5) with an optimum temperature of 55 degrees C. Compared with the major commercial phytases from Aspergillus niger, Escherichia coli, and a potential commercial phytase from Y. intermedia, the Y. rohdei phytase was more resistant to pepsin, retained more activity under gastric conditions, and released more inorganic phosphorus (two to ten times) from soybean meal under simulated gastric conditions. These superior properties suggest that the Y. rohdei phytase is an attractive additive to animal feed. Our study indicated that, in order to better hydrolyze the phytate and release more inorganic phosphorus in the gastric passage, phytase should have high activity and stability, simultaneously, at low pH and high protease concentration.
Appl Microbiol Biotechnol 2008 Sep
PMID:A novel phytase from Yersinia rohdei with high phytate hydrolysis activity under low pH and strong pepsin conditions. 1854 46

The role of disulfide bridges in the folding of Aspergillus niger phytase pH 2.5-optimum (PhyB) was investigated using dynamic light scattering (DLS). Guanidinium chloride (GuCl) at 1.0 M unfolded phytase; however, its removal by dialysis refolded the protein. The thiol reagent tris(2-carboxyethyl)phosphine (TCEP) reduces the refolding activity by 68%. The hydrodynamic radius (R(H)) of PhyB phytase decreased from 5.5 to 4.14 nm when the protein was subjected to 1.0 M GuCl concentration. The active homodimer, 183 kDa, was reduced to a 92 kDa monomer. The DLS data taken together with activity measurements could indicate whether refolding took place or not in PhyB phytase. The correlation between molecular mass and the state of unfolding and refolding is a very strong one in fungal phytase belonging to histidine acid phosphatase (HAP). Unlike PhyA phytase, for which sodium chloride treatment boosted the activity at 0.5 M salt concentration, PhyB phytase activity was severely inhibited under identical condition. Thus, PhyA and PhyB phytases are structurally very different, and their chemical environment in the active site and substrate-binding domain may be different to elicit such an opposite reaction to monovalent cations.
J Agric Food Chem 2008 Sep 10
PMID:Unfolding and refolding of Aspergillus niger PhyB phytase: role of disulfide bridges. 1868 44

LC-MS technique described here is a new way for the separation and direct determination of UV-Vis insensitive inositol phosphates (InsP(2)-InsP(6)). This circumvents the need of radioisotopic labeling and post-column derivatization techniques. The method involves separation of various enzymatically dephosphorylated derivatives of InsP(6) on C(18)-column using MeOH/H(2)O (30:70 v/v) and their identification using electron spray ionization MS in positive ion mode (+pESI-MS). The LC-MS studies revealed that the purified phytase from Aspergillus niger van Teighem hydrolyzes InsP(6 )in a sequential manner leading to InsP(2 )(InsP(2) x 2Na, t(R) 4.4-4.54 min, base peak m/z 382.9) as the end product.
J Sep Sci 2008 Dec
PMID:Separation and identification of enzymatically prepared dephosphorylated products of myo-inositolhexakisphosphate using LC-MS. 1900 37


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