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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)

Ninety hens were divided into six groups as a 2 x 3 factorial design and fed diets containing Wheat Bran (WB) at two levels of 0 and 5% and the enzyme phytase at three levels of 0, 150 and 300 FTU kg(-1). Egg weight, egg production, feed intake and Feed Conversion Ratio (FCR) were determined. Eggs were collected on two consecutive days at fortnightly intervals to measure egg size and egg component weights. Shell thickness was measured. Egg production, egg weight, FCR and feed intake were not affected by WB. Egg production, egg weight and feed intake were significantly higher in phytase-supplemented groups than unsupplemented groups. FCR differed significantly between dietary treatments as phytase supplementation significantly decreased FCR. Inclusion of WB to the diets had no effect on egg size and albumen weight. Phytase supplementation did not affect yolk weight, although albumen and shell weight were significantly affected.
Pak J Biol Sci 2008 Sep 15
PMID:Performance and egg quality of laying hens affected by different sources of phytase. 1913 43

Low phosphorus (P) availability is a major constraint to crop growth and production, including soybean (Glycine max), on a global scale. However, 50% to 80% of the total P in agricultural soils exists as organic phosphate, which is unavailable to plants unless hydrolyzed to release inorganic phosphate. One strategy for improving crop P nutrition is the enhanced activity of acid phosphatases (APases) to obtain or remobilize inorganic phosphate from organic P sources. In this study, we overexpressed an Arabidopsis (Arabidopsis thaliana) purple APase gene (AtPAP15) containing a carrot (Daucus carota) extracellular targeting peptide in soybean hairy roots and found that the APase activity was increased by 1.5-fold in transgenic hairy roots. We subsequently transformed soybean plants with AtPAP15 and studied three homozygous overexpression lines of AtPAP15. The three transgenic lines exhibited significantly improved P efficiency with 117.8%, 56.5%, and 57.8% increases in plant dry weight, and 90.1%, 18.2%, and 62.6% increases in plant P content, respectively, as compared with wild-type plants grown on sand culture containing phytate as the sole P source. The transgenic soybean lines also exhibited a significant level of APase and phytase activity in leaves and root exudates, respectively. Furthermore, the transgenic lines exhibited improved yields when grown on acid soils, with 35.9%, 41.0%, and 59.0% increases in pod number per plant, and 46.0%, 48.3%, and 66.7% increases in seed number per plant. Taken together, to our knowledge, our study is the first report on the improvement of P efficiency in soybean through constitutive expression of a plant APase gene. These findings could have significant implications for improving crop yield on soils low in available P, which is a serious agricultural limitation worldwide.
Plant Physiol 2009 Sep
PMID:Overexpressing AtPAP15 enhances phosphorus efficiency in soybean. 1958 3

Purple acid phosphatase (PAP) catalyzes the hydrolysis of phosphate monoesters and anhydrides to release phosphate within an acidic pH range. Among the 29 PAP-like proteins in Arabidopsis (Arabidopsis thaliana), AtPAP15 (At3g07130) displays a greater degree of amino acid identity with soybean (Glycine max; GmPHY) and tobacco (Nicotiana tabacum) PAP (NtPAP) with phytase activity than the other AtPAPs. In this study, transgenic Arabidopsis that expressed an AtPAP15 promoterbeta-glucuronidase (GUS) fusion protein showed that AtPAP15 expression was developmentally and temporally regulated, with strong GUS staining at the early stages of seedling growth and pollen germination. The expression was also organ/tissue specific, with strongest GUS staining in the vasculature, pollen grains, and roots. The recombinant AtPAP purified from transgenic tobacco exhibited broad substrate specificity with moderate phytase activity. AtPAP15 T-DNA insertion lines exhibited a lower phytase and phosphatase activity in seedling and germinating pollen and lower pollen germination rate compared with the wild type and their complementation lines. Therefore, AtPAP15 likely mobilizes phosphorus reserves in plants, particularly during seed and pollen germination. Since AtPAP15 is not expressed in the root hair or in the epidermal cells, it is unlikely to play any role in external phosphorus assimilation.
Plant Physiol 2009 Sep
PMID:Molecular and biochemical characterization of AtPAP15, a purple acid phosphatase with phytase activity, in Arabidopsis. 1963 33

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.
J Biosci Bioeng 2009 Sep
PMID:Cloning and characterization of a novel phytase from wastewater treatment yeast Hansenula fabianii J640 and expression in Pichia pastoris. 1966 57

Combining ease of genetic manipulation and fermentation with the ability to secrete and to glycosylate proteins in the basic eukaryotic manner, Arxula adeninivorans provides an attractive expression platform. Based on a redesign of the basic vector, a new Arxula vector system, Xplor 2, for heterologous gene expression was established, which allows (1) the construction of expression plasmids for supertransformation of A. adeninivorans strains secreting target proteins of biotechnological interest and (2) the integration of small vector cassettes consisting of yeast DNA sequences only. For this purpose, a set of modules including the ATRP1m selection-marker module, expression modules for constitutive expression of the genes phyK (Klebsiella-derived phytase) and IFNalpha2a (human interferon alpha), the HARS (Hansenula polymorpha autonomous replication sequence) for autonomous replication and the chaperone module AHSB4 promoter -HpCNE1 gene (calnexin) -PHO5 terminator to improve secretion efficiency were constructed and integrated in various combinations in the basic vector Xplor 2. After removal of the complete Escherichia coli-based plasmid parts (resistance marker, ColE1 ori and f1(-) origin), the remaining yeast-based linear vector fragment with or without rDNA targeting sequences were transformed as yeast rDNA integrative expression cassettes and yeast integrative expression cassettes (YICs), respectively, and the resulting strains were tested for their capacity to secrete PhyK or IFNalpha2a. Maximal expression levels were consistently obtained using YICs for transformation irrespective of whether or not they carry HARS and/or calnexin modules. It is recommended that at least 50 such transformants be analyzed to ensure selection of the best transformants.
Appl Microbiol Biotechnol 2009 Sep
PMID:Xplor 2--an optimized transformation/expression system for recombinant protein production in the yeast Arxula adeninivorans. 1967 89

One experiment was conducted to investigate the benefits of a multi-enzyme complex, containing carbohydrases (from Penicillium funiculosum) and phytase (bacterial 6-phytase) activities, on the performance and bone mineralization of broiler chickens fed corn-soybean meal diets. A total of 2,268 male broilers were allocated to 9 treatments, replicated 6 times, in a randomized complete block design from 1 to 43 d. A positive control (PC) diet formulated to be adequate in nutrients and 4 reduced nutrient diets (NC1 to NC4), with gradual decrease on AME, CP, and digestible amino acids (CP-dAA) and available P (avP) and Ca contents, with or without enzyme supplementation, were tested. The nutrient reductions applied were NC1 (-65 kcal/kg, -1.5% CP-dAA) and NC2 (-85 kcal/kg, -3.0% CP-dAA) both with -0.15 percent point avP and -0.12 percent point Ca and NC3 (-65 kcal/kg, -1.5% CP-dAA) and NC4 (-85 kcal/kg, -3.0% CP-dAA) both with -0.20 percent point avP and -0.16 percent point Ca. Supplementation of the NC diets with the enzyme complex increased ADFI (P<0.001), ADG (P<0.001), and reduced feed:gain (P<0.01). The magnitude of the enzyme effect in increasing feed intake and weight gain was greater for the diets with greatest reductions in avP and Ca. Enzyme supplementation increased (P<0.001) feed intake of birds fed on NC diets close to the level of feed consumption of the PC. Enzyme supplementation to NC diets resulted in all cases in lower (P<0.05) feed:gain than the PC. Enzyme supplementation to NC1 and NC3 diets restored bone mineralization to that of the PC, whereas ash and Ca with NC2 and NC4 diets and P with NC4 diet remained lower (P<0.05). These results suggest that the dietary supplementation with a multi-enzyme complex containing nonstarch polysaccharide enzymes and phytase is efficient in reducing the P, energy, protein, and amino acid specifications of corn-soybean meal diets.
Poult Sci 2009 Sep
PMID:Enzyme complex containing carbohydrases and phytase improves growth performance and bone mineralization of broilers fed reduced nutrient corn-soybean-based diets. 1968 77

In the eukaryotic cell, protein glycosylation takes place in the crowded environment of the endoplasmatic reticulum. With the purpose of elucidating the impact of high concentration on the interactions of glycoproteins, we have conducted a series of small-angle x-ray scattering experiments on the heavily glycosylated enzyme Peniophora lycii phytase (Phy) and its deglycosylated counterpart (dgPhy). The small-angle x-ray scattering data were analyzed using an individual numerical form factor for each of the two glycoforms combined with two structure factors, a hard sphere and a screened coulomb potential structure factor, respectively, as determined by ab initio analysis. Based on this data analysis, three main conclusions could be drawn. First, at comparable protein concentrations (mg/ml), the relative excluded volume of Phy was approximately 75% higher than that of dgPhy, showing that the glycans significantly increase excluded-volume interactions. Second, the relative excluded volume of dgPhy increased with concentration, as expected; however, the opposite effect was observed for Phy, where the relative excluded volume decreased in response to increasing protein concentration. Third, a clear difference in the effect of salinity on the excluded-volume interactions was observed between the two glycol forms. Although the relative excluded volume of dgPhy decreased with increasing ionic strength, the relative excluded volume of Phy was basically insensitive to increased salinity. We suggest that protrusion forces from the glycans contribute to steric stabilization of the protein, and that glycosylation helps to sustain repulsive electrostatic interactions under crowded conditions. In combination, this aids in stabilizing high concentrations of glycosylated proteins.
Biophys J 2009 Sep 02
PMID:Interrelationship of steric stabilization and self-crowding of a glycosylated protein. 1972 33

1. Caecectomised laying hens were used in two assays to study the effects of a microbial 6-phytase on amino acid (AA) digestibility and energy metabolisability using (1) diets with phytate-rich protein sources and (2) with two dietary phosphorus (P) levels. The two assays followed a 2 x 2-factorial arrangement of treatments using 8 hens per treatment. The hens were housed individually in metabolism cages, and excreta were quantitatively collected for a period of 5 d. 2. In Assay 1, two dietary P levels (8.0 and 4.0 g/kg dry matter) and two levels of phytase supplementation (0 and 1000 U/kg diet) were used in diets that were mainly based on maize, sunflower meal and wheat gluten. The digestibility of AA was 001 to 002 lower in the diet with the low P than with the high P concentration. The effect of P content was significant for 12 out of the 14 AA studied. The supplementation of phytase significantly improved the degradation of myo-inositol(1,2,3,4,5,6)hexakisphosphate (IP6), but affected neither AA digestibility nor energy metabolisability. An interaction between the two factors was not detected. 3. In Assay 2, diets contained one main protein source (sunflower meal or rapeseed meal) at a concentration of 250 g/kg. The diets were either supplemented or not with phytase (1500 U/kg diet). On average, AA digestibility was 0.01 lower in the rapeseed meal-containing diet than in the sunflower meal-containing one. The maximum difference was 0.03. The effect of the protein source was significant for 9 of the 14 AA studied. The supplementation of phytase had no significant effect on AA digestibility or energy metabolisability. 4. Our studies do not substantiate the hypothesis that improved IP6 degradation due to phytase supplementation is associated with improved AA digestibility and energy metabolisability in laying hens. An interaction between phytase efficacy to improve AA digestibility or energy metabolisability and the P level in the diet does not seem to exist.
Br Poult Sci 2009 Sep
PMID:Studies on the effects of microbial phytase on amino acid digestibility and energy metabolisability in caecectomised laying hens and the interaction with the dietary phosphorus level. 1990 37

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.
Br Poult Sci 2009 Sep
PMID:Previous exposure to dietary phytase reduces the endogenous energy losses from precision-fed chickens. 1990 39

Porcine liver proteome iTRAQ analysis enabled the confident identification of 880 proteins with a rate of false positive identifications of less than 5%. Proteins involved in energy metabolism, catabolism, protein biosynthesis, electron transport, and other oxidoreductase reactions were highly enriched confirming the central role of liver as the major chemical and energy factory. Comparative analysis with human and mouse liver proteomes demonstrated that 80% of proteins were common to all three liver proteomes. In addition, it was also demonstrated that both sex of the animal and introduction of a novel phytase transgene into the genome each affected around 5% of total liver proteome. After controlling the false discovery rate (FDR</=0.1) using the Storey q value only four proteins (EPHX1, CAT, PAH, ST13) were shown to be differentially expressed between genders (Males/Females) and two proteins (SELENBP2, TAGLN) were differentially expressed between two lines (Transgenic/Conventional pigs). Current analysis is the largest proteome analysis for pig and complements the more extensive human and mouse proteome projects.
Comp Biochem Physiol Part D Genomics Proteomics 2008 Sep
PMID:Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines. 2048 22


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