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At least 19 recordsLinked to original sources
PubMed2004

Effects of combining three fungal phytases with a bacterial phytase on plasma phosphorus status of weanling pigs fed a corn-soy diet.

The objective of this study was to determine possible synergistic effects of supplementing one of three fungal phytases: Aspergillus fumitagus PhyA (AFP),A. niger PhyA (ANP), or Peniophora lyci phytase (PLP) with an Escherichia coli AppA phytase (EP) in diets for pigs. Three experiments, each lasting for 4 wk, were conducted with a total of 106 weanling pigs (5 wk old). The corn-soybean meal basal diet (BD) contained no supplemental inorganic P. In Exp. 1, 35 pigs (8.6 +/- 1.0 kg BW) were fed (as-fed basis) BD + AFP at 750 U/ kg of feed, BD + inorganic P (0.2% P), or BD + PLP at 500, 750, or 1,000 U/kg feed. Pigs fed BD + AFP or BD + 0.2% P had higher (P < 0.05) plasma inorganic P concentrations than those fed BD + PLP at the end of the trial (wk 4). In Exp. 2, 35 pigs (8.1 +/- 0.9 kg BW) were fed BD + AFP, EP, PLP, a 1:1 mix of AFP:EP, or a 1:1 mix of PLP:EP at 500 U/kg. Pigs fed the AFP:EP mixture had growth performance and plasma measures similar to those fed either enzyme alone. Pigs fed the PLP:EP mixture had lower (P < 0.05) plasma alkaline phosphatase activity than those fed BD + PLP. Pigs fed BD + PLP had lower (P < 0.05) plasma inorganic P concentrations than pigs fed BD + EP, and higher (P < 0.05) plasma alkaline phosphatase activity than all other groups at wk 4. In Exp. 3, 36 pigs (9.1 +/- 1.2 kg BW) were fed BD + ANP, EP, or a 1:1 mix of ANP:EP at 500 U/kg feed. Pigs fed the two enzymes together had lower (P < 0.05) plasma inorganic P concentration than those fed BD + EP and lower (P < 0.05) plasma alkaline phosphatase activity than pigs fed BD + ANP at wk 4. In conclusion, although the four phytases showed different effects on plasma P status of weanling pigs, there was no synergistic effect between any of the three fungal phytases and the bacterial phytase on the plasma measures or growth performance under the conditions of the present study.

6-Phytase↗
PubMed2026

In silico genome mining and characterization of putative horse feces-derived bacterial phytases as potential monogastric animal feed additive candidates.

Phytic acid exerts a significant antinutritional effect in poultry, swine, and fish, which can be mitigated by supplementing monogastric feeds with efficient microbial phytases. Accordingly, mining bacterial genomes for novel phytases represents a strategic computational approach to identifying candidates for improving monogastric animal nutrition. In this study, 162 bacterial genomes associated with horse feces were systematically mined using an in silico pipeline to identify and characterize putative phytases.A total of 69 non-redundant sequences were identified and classified as histidine acid phytase (HAPhy) or protein tyrosine phosphatase-like phytase (PTPLPhy). HAPhys were detected in the genomes of Escherichia coli, Klebsiella pneumoniae, Salmonella enterica, Acinetobacter baumannii, and Cutibacterium equinum, whereas PTPLPhys were found in K. pneumoniae, Limosilactobacillus reuteri, Pediococcus acidilactici, Bifidobacterium pseudolongum, and Prescottella equi. Principal component analysis identified glucose-1-phosphatase (CAJ1242485.1) and bifunctional acid phosphatase (NHR17779.1) as the HAPhy candidates exhibiting the most favorable predicted physicochemical properties for potential feed applications. Similarly, among the PTPLPhys, protein tyrosine phosphatase (UNQ40438.1) and a hypothetical protein (CAJ1246072.1) showed the most favorable computational profiles. Biosafety analysis identified potential virulence factors, indicating that sources should be screened prior to feed application. High-quality AlphaFold2 models were obtained for these phytases (90.9-97.2). Molecular docking analysis showed that NHR17779.1 exhibited the strongest binding to phytic acid, whereas CAJ1246072.1 demonstrated the weakest interaction. Overall, this study identifies the horse fecal microbiota as a diverse source of putative phytases that may serve as promising targets for genetic and protein engineering; however, further in vitro and in vivo studies are essential to validate the enzymatic activity and industrial efficacy of these computational candidates.

Bacterial phytase↗
PubMed2004

[Phytase activity in some groups of bacteria. Search for and cloning of genes for bacterial phytases].

A search for phytase genes in 9 Bacillus strains from the collection of IMGAN was implemented. The growth optimum of strains IX-22, IX-12B, K17-2, K18, IMG I, IMG II, M4 and M8 was 50-60 degrees C; the optimal growth temperature for Bacillus sp. 790 was 45-47 degrees C. According to the sequence data of 16S RNA genes, Bacillus sp. 790 belongs to the B. subtilis/amyloliquefaciens group. The other 8 strains were identified as B. licheniformis. Selection of Bacillus strains, potentially containing the phytase genes, was performed via PCR with primers designed on the basis of the conserved sequence regions of the phyA gene from B. amyloliquefaciens FZB45 with chromosomal DNA being used as the template. The nucleotide sequences of all PCR fragments showed a high level of homology to the known Bacillus phytase genes. The gene libraries of B. licheniformis M8 and B. amyloliquefaciens 790 in E. coli were constructed and phytase-containing clones were selected from them. Twenty-four Pseudomonas strains of different species, 5 Xanthomonas maltophilia strains and 1 Xanthomonas malvacearum (all from the mentioned collection) were tested for phytase activity. Such activity was found in 13 Pseudomonas strains and in 6 Xanthomonas strains. The accumulation of phytase in Pseudomonas was shown to take place at later (over 2 days') growth stages. The optimum pH for phytase from 3 Pseudomonas strains were established. The enzymes were found to be most active at pH 5.5.

6-Phytase↗
PubMed2003

Optimization of the extracellular production of a bacterial phytase with Escherichia coli by using different fed-batch fermentation strategies.

The extracellular production of Escherichia coli phytase was studied in fed-batch fermentations. Two different feeding strategies were compared: control by keeping the glucose concentration constant, and control by keeping a low constant oxygen level in the medium. For the feeding control based on glucose concentration, a recently developed rapid glucose controlling system was tested for the first time in bacterial cultivations and used to establish the fermentative production of extracellular phytase with E. coli. High activity levels (120 U ml(-1)) at short cultivation times (14 h) were obtained. Even higher activity levels - albeit at longer cultivation times - were reached by applying a feeding control, the main characteristic of which was a constant low oxygen concentration. The optimum oxygen level for the production of phytase was in the range of 5-10% saturation.

6-Phytase↗
PubMed2004

Production of two highly active bacterial phytases with broad pH optima in germinated transgenic rice seeds.

Phytate is the main storage form of phosphorus in many plant seeds, but phosphate bound in this form is not available to monogastric animals. Phytase, an enzyme that hydrolyzes phosphate from phytate, has the potential to enhance phosphorus availability in animal diets when engineered in rice seeds as a feed additive. Two genes, derived from a ruminal bacterium Selenomonas ruminantium (SrPf6) and Escherichia coli (appA), encoding highly active phytases were expressed in germinated transgenic rice seeds. Phytase expression was controlled by a germination inducible alpha-amylase gene (alphaAmy8) promoter, and extracellular phytase secretion directed by an betaAmy8 signal peptide sequence. The two phytases were expressed in germinated transgenic rice seeds transiently and in a temporally controlled and tissue-specific manner. No adverse effect on plant development or seed formation was observed. Up to 0.6 and 1.4 U of phytase activity per mg of total extracted cellular proteins were obtained in germinated transgenic rice seeds expressing appA and SrPf6 phytases, respectively, which represent 46-60 times of phytase activities compared to the non-transformant. The appA and SrPf6 phytases produced in germinated transgenic rice seeds had high activity over broad pH ranges of 3.0-5.5 and 2.0-6.0, respectively. Phytase levels and inheritance of transgenes in one highly expressing plant were stable over four generations. Germinated transgenic rice seeds, which produce a highly active recombinant phytase and are rich in hydrolytic enzymes, nutrients and minerals, could potentially be an ideal feed additive for improving the phytate-phosphorus digestibility in monogastric animals.

6-Phytase↗
PubMed2001

Transgenic mice expressing bacterial phytase as a model for phosphorus pollution control.

We have developed transgenic mouse models to determine whether endogenous expression of phytase transgenes in the digestive tract of monogastric animals can increase the bioavailability of dietary phytate, a major but indigestible form of dietary phosphorus. We constructed phytase transgenes composed of the appA phytase gene from Escherichia coli regulated for expression in salivary glands by the rat R15 proline-rich protein promoter or by the mouse parotid secretory protein promoter. Transgenic phytase is highly expressed in the parotid salivary glands and secreted in saliva as an enzymatically active 55 kDa glycosylated protein. Expression of salivary phytase reduces fecal phosphorus by 11%. These results suggest that the introduction of salivary phytase transgenes into monogastric farm animals offers a promising biological approach to relieving the requirement for dietary phosphate supplements and to reducing phosphorus pollution from animal agriculture.

6-Phytase↗
PubMed2006

Cloning of pig parotid secretory protein gene upstream promoter and the establishment of a transgenic mouse model expressing bacterial phytase for agricultural phosphorus pollution control.

This study examined the feasibility of using the promoter of the pig parotid secretory protein (PSP) gene for expression of the phytase transgene in mouse models. The pig parotid secretory protein gene is specifically expressed at high levels in the salivary glands. The 10-kb upstream promoter region of the gene necessary for tissue-specific expression has been identified. We have constructed phytase transgenes composed of the appA phytase gene from Escherichia coli driven by the upstream promoter region of the pig PSP gene with a 3' tail of either bovine growth hormone or the pig PSP gene polyadenylation signal. Transgenic mouse models with the construct showed that the upstream region of the pig PSP gene is sufficient for directing the expression of phytase transgenes in the saliva. Expression of salivary phytase reduced fecal phytate by 8.5 and 12.5% in 2 transgenic mouse lines, respectively. These results suggest that the expression of phytase in salivary glands of monogastric animals offers a promising biological approach to relieve the requirement for dietary phosphate supplements and to reduce phosphorus pollution from animal agriculture.

6-Phytase↗
PubMed2002

Efficacy of supplementation of a phytase-producing bacterial culture on the performance and nutrient use of broiler chickens fed corn-soybean meal diets.

We evaluated the efficacy of supplementation of active Mitsuokella jalaludinii culture (AMJC) on the growth performance, nutrient use, and mineral concentrations in tibia bone and plasma of broiler chickens fed corn-soybean meal diets. Dietary treatments included low-nonphytate P (NPP) feed (containing 0.24% and 0.232% NPP for chicks from 1 to 21 and 22 to 42 d of age, respectively), low-NPP feed added with different levels of AMJC (equivalent to 250, 500, 750, and 1,000 U phytase/kg of feed), and normal-NPP feed (containing 0.46 and 0.354% NPP for chicks from 1 to 21 and 22 to 42 d of age, respectively). Supplementation of AMJC to low-NPP feed increased (P < 0.05) weight gain and feed intake and decreased (P < 0.05) feed:gain ratio of chickens during the whole experiment (Days 1 to 42). Supplementation of AMJC increased (P < 0.05) the AME value, digestibility of DM and CP, and retention of P, Ca, and Cu. Mn retention in broilers was only increased (P < 0.05) by AMJC supplementation from 18 to 20 d of age, and Zn retention was improved (P < 0.05) only at a high level of AMJC (equivalent to 1,000 U phytase/kg of feed) supplementation. Chicks fed low-NPP feed added with AMJC had similar tibia ash percentages as those fed the normal-NPP diet. Generally, supplementing AMJC to low-NPP feed increased (P < 0.05) Ca, decreased significantly (P < 0.05) Mn and Cu, but did not affect Zn and P concentrations in tibia ash. Supplementing AMJC also increased (P < 0.05) plasma P but had no effect on plasma Ca or Mn. Plasma Zn concentration was increased only when a high level of AMJC (equivalent to 1,000 U phytase/kg of feed) was used. In conclusion, AMJC supplementation to low-NPP feed improved growth performance; AME value; digestibility of CP and DM; use of Ca, P, and Cu; and bone mineralization.

6-Phytase↗
PubMed1999

Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain.

A novel bacterial phytase from a Bacillus amyloliquefaciens strain was crystallized using the hanging-drop vapour-diffusion method. The amino-acid sequence of the enzyme does not show any homology to those of other known phytases or phosphatases, with the exception of a phytase from Bacillus subtilis. The enzyme exhibits a thermal stability which is strongly dependent on calcium ions. High-quality single crystals of the enzyme in the absence of calcium ions were obtained using a precipitant solution containing 20% 2-methyl-2, 4-pentanediol and 0.1 M MES (pH 6.5). Native diffraction data to 2.0 A resolution were obtained from a flash-frozen crystal at 110 K using a rotating-anode X-ray source. The crystals belong to space group P212121 with unit-cell dimensions a = 50.4, b = 64.1, c = 104. 2 A and contain one monomer per asymmetric unit. Structure determination using heavy-atom derivative crystals is in progress, along with an effort to crystallize the calcium ion bound form of the enzyme.

6-Phytase↗
PubMed2026

A culturomics approach reveals cross-feeding capacity of intestinal pig bacteria upon release of inositol from phytate.

BACKGROUND: Phytate is the primary phosphorus storage molecule of plants and plays a major role in animal nutrition. To enhance phosphate availability and absorption in livestock, and to reduce eutrophication by liquid manure, bacterial phytases are often added to animal feed. The dephosphorylated form of phytate, the polyol myo-inositol (myo-Ins) with multiple functions in eukaryotes, is metabolized by approximately 30% of all bacterial species. RESULTS: Here, we employed a culturomics approach to identify possible metabolic interactions between phytase-producing and myo-Ins degrading bacteria in intestinal samples from pigs. Selective cultivation revealed an unexpectedly high abundance of myo-Ins degrading bacteria, suggesting substantial phytate dephosphorylation in the pig gut. Phytase activity assays performed on gut isolates showed a high degree of variability, suggesting the presence of a diverse set of phytases yet to be characterized. Furthermore, using supernatants of phytase-positive gut strains cultivated in the presence of phytate, we observed cross-feeding of myo-Ins from phytase producers to phytase-negative strains, including the pathogen Salmonella enterica serovar Typhimurium. CONCLUSIONS: The data demonstrate that a wide range of commensal bacteria can potentially benefit from phytase activity by utilizing myo-Ins, released through phytate hydrolysis, as a growth substrate. Video Abstract.

Animals↗
PubMed2004

Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement.

The inclusion of phytase in monogastric animal feed has the benefit of hydrolyzing indigestible plant phytate (myo-inositol 1,2,3,4,5,6-hexakis dihydrogen phosphate) to provide poultry and swine with dietary phosphorus. An ideal phytase supplement should have a high temperature tolerance, allowing it to survive the feed pelleting process, a high specific activity at low pHs, and adequate gastric performance. For this study, the performance of a bacterial phytase was optimized by the use of gene site saturation mutagenesis technology. Beginning with the appA gene from Escherichia coli, a library of clones incorporating all 19 possible amino acid changes and 32 possible codon variations in 431 residues of the sequence was generated and screened for mutants exhibiting improved thermal tolerance. Fourteen single site variants were discovered that retained as much as 10 times the residual activity of the wild-type enzyme after a heated incubation regimen. The addition of eight individual mutations into a single construct (Phy9X) resulted in a protein of maximal fitness, i.e., a highly active phytase with no loss of activity after heating at 62 degrees C for 1 h and 27% of its initial activity after 10 min at 85 degrees C, which was a significant improvement over the appA parental phytase. Phy9X also showed a 3.5-fold enhancement in gastric stability.

6-Phytase↗
PubMedDate not supplied

Utilisation of phytate phosphorus by rumen bacteria in a semi-continuous culture system (Rusitec) in lactating goats fed on different forage to concentrate ratios.

Experimental data on phytate phosphorus utilisation by ruminants are scarce. The aim of this study was to estimate the phytase activity of rumen micro-organisms when phytate phosphorus supply is high. A semi-continuous culture system fermentor (RUSITEC) was used. The inoculum was obtained from eight goats fed on either high or low forage level diets. Experimental buffers only differed by the nature of phosphorus monosodium phosphate vs. corn sodium phytate. The nylon bags containing 15 g DM of substrate were removed after a 48-hour incubation period. The system was maintained for 15 days: 5 days for adaptation, in order to obtain a steady state, and 10 days for sampling and recording. No significant differences were observed for DM digestibility, gas production, pH, N-NH3, and SCFA for the different treatments. Bacterial efficiency of phytate phosphorus utilisation was significantly higher (p < 0.001) with organic P, but remained lower than the data usually reported in the literature. These results may be explained by the relative saturation of bacterial phytase activity when the buffer contains a high level of phytate phosphorus.

Animal Feed↗
PubMed1997

Purification and characterization of a phytase from Klebsiella terrigena.

A cytoplasmatic phytase was purified about 410-fold to apparent homogeneity with a recovery of 28%. The enzyme is induceable under carbon limitation in the presence of phytate. It behaves as a monomeric protein of a molecular mass of about 40 kDa. The phytase is rather specific for phytate and exhibits optimal conditions for phytate degradation at pH 5.0 and 58 degrees C. Kinetic parameters for the hydrolysis of Na phytate are KM 300 microM and kcat 180 s-1 at 35 degrees C and pH 5.0. Phytate is hydrolyzed in a stepwise manner; the penta- and tetrakisphosphate were identified as I(1,2,4,5,6)P5 and I(1,2,5,6)P4. Consequently, this enzyme is a 3-phytase (EC 3.1.3.8).

6-Phytase↗
PubMed1998

Purification, crystallization and preliminary X-ray analysis of the Escherichia coli phytase.

A recombinant form of Escherichia coli phytase, which hydrolyzes phytic acid into phosphate and myo-inositol, has been expressed, purified and crystallized. Crystals have been obtained by the method of bulk crystallization in 10 mM sodium acetate buffer (pH 4.5) without using a conventional precipitant. The enzyme crystallized in space group P21, with unit-cell dimensions a = 74.9, b = 72.2, c = 82.4 A, and beta = 92.0 degrees. Crystals diffract to at least 2.2 A at a rotating-anode X-ray source and a 2.3 A resolution data set has been collected, giving completeness of 98.0% and an Rsym of 0.072. Assuming there are two phytase molecules in the asymmetric unit, the solvent content is calculated to be 42.1%. A self-rotation function shows a clear twofold non-crystallographic symmetry relating two molecules of E. coli phytase in the asymmetric unit.

6-Phytase↗
PubMed2002

Regulation of Raoultella terrigena comb.nov. phytase expression.

Phytases catalyze the release of phosphate from phytate (myo-inositol hexakisphosphate) to inositol polyphosphates. Raoultella terrigena comb.nov. phytase activity is known to increase markedly after cells reach the stationary phase. In this study, phytase activity measurements made on single batch cultures indicated that specific enzyme activity was subject to catabolite repression. Cyclic AMP (cAMP) showed a positive effect in expression during exponential growth and a negative effect during stationary phase. RpoS exhibited the opposite effect during both growth phases; the induction to stationary phase decreased twofold in the rpoS::Tn10 mutant, but the effect of RpoS was not clearly determined. Two phy::MudI1734 mutants, MW49 and MW52, were isolated. These formed small colonies in comparison with the MW25 parent strain when plated on Luria-Bertani (LB) or LB supplemented with glucose. They did not grow in minimal media or under anaerobiosis, but did grow aerobically on LB and LB glucose at a lower rate than did MW25. The beta-galactosidase activity level in these mutants increased three to four fold during stationary growth in LB glucose and during anaerobiosis. Addition of cAMP during the exponential growth of MW52 on LB glucose provoked a decrease in beta-galactosidase activity during the stationary phase, confirming its negative effect on phytase expression during stationary growth.

6-Phytase↗