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 full-length cDNA encoding an extracellular form of phytase was isolated from the model legume Medicago truncatula. The phytase cDNA (MtPHY1) has an open reading frame of 1,632 bp predicted to encode 543 amino acids including an N-terminal signal peptide of 27 amino acids. The MtPHY1 gene is 5,151 bp in length, containing 7 exons and 6 introns. MtPHY1 transcripts were detected in leaves and roots and levels elevated in roots during growth in low phosphate conditions. Transgenic Arabidopsis lines expressing MtPHY1 under the control of the root-specific MtPT1 promoter or the constitutive CaMV35S promoter were created. Phytase activities in root apoplast of the transgenic Arabidopsis were 12.3- to 16.2-fold higher than those of the control plants. The expressed phytase was secreted into the rhizosphere as demonstrated by enzyme activity staining and HPLC analysis of phytate degradation by root exudates. Transgenic expression of the MtPHY1 led to significant improvement in organic phosphorus utilization and plant growth. When phytate was supplied as the sole source of phosphorus, dry weight of the transgenic Arabidopsis lines were 3.1- to 4.0-fold higher than the control plants and total phosphorus contents were 4.1- to 5.5-fold higher than the control. Transgenic expression of phytase genes of plant origin has great potential for improving plant phosphorus acquisition and for phytoremediation.
Planta 2005 Sep
PMID:Transgenic expression of a novel M. truncatula phytase gene results in improved acquisition of organic phosphorus by Arabidopsis. 1585 83

Phytases decompose phytate, which is the primary storage form of phosphate in plants. More than 10 years ago, the first commercial phytase product became available on the market. It offered to help farmers reduce phosphorus excretion of monogastric animals by replacing inorganic phosphates by microbial phytase in the animal diet. Phytase application can reduce phosphorus excretion by up to 50%, a feat that would contribute significantly toward environmental protection. Furthermore, phytase supplementation leads to improved availability of minerals and trace elements. In addition to its major application in animal nutrition, phytase is also used for processing of human food. Research in this field focuses on better mineral absorption and technical improvement of food processing. All commercial phytase preparations contain microbial enzymes produced by fermentation. A wide variety of phytases were discovered and characterized in the last 10 years. Initial steps to produce phytase in transgenic plants were also undertaken. A crucial role for its commercial success relates to the formulation of the enzyme solution delivered from fermentation. For liquid enzyme products, a long shelf life is achieved by the addition of stabilizing agents. More comfortable for many customers is the use of dry enzyme preparations. Different formulation technologies are used to produce enzyme powders that retain enzyme activity, are stable in application, resistant against high temperatures, dust-free, and easy to handle.
Appl Microbiol Biotechnol 2005 Sep
PMID:Biotechnological production and applications of phytases. 1604 77

Supplementation of microbial phytase usually improves the digestibility and utilization of phosphorus in feedstuffs of plant origin. The effect of phytase supplementation on the digestibilities of AA also has been examined, but the results have been inconsistent. This study was carried out to determine the effect of phytase (Natuphos) supplementation, at a rate of 2,000 phytase units/kg, to two basal diets on the apparent ileal digestibilities (AID) of GE, CP, and AA, and on the apparent total-tract digestibilities (ATTD) of CP and GE. The basal diets contained 18% CP and were formulated (as-fed basis) to contain either a low (0.22%) or high content (0.48%) of phytate P. The high-phytate diet contained 20% rice bran, which is a rich source of phytate and has low intrinsic phytase activity. Eight barrows (average initial BW = 40.6 kg), fitted with a simple T-cannula at the distal ileum, were fed the four diets according to a replicated 4 x 4 Latin square design. The pigs were fed twice daily at 0800 and 2000, equal amounts each meal, at a rate of 2.4 times the daily maintenance requirement for ME. Each experimental period comprised 14 d. Ileal digesta were collected from 0800 to 2000 on d 12, 13, and 14. Feces were collected from 0800 on d 8 until 0800 on d 12. Chromic oxide was used as the digestibility marker. The AID of GE, CP, and AA and the ATTD of CP and GE were less in the high- than in the low-phytate diet (P < 0.01). With the exception of glutamic acid, phytase supplementation did not affect (P > 0.10) the AID of CP and AA. There was no effect (P > 0.05) of phytase on the ATTD of CP and GE. These results show that if a response occurs to phytase supplementation, it is independent of the dietary phytate content.
J Anim Sci 2005 Sep
PMID:Effect of phytase supplementation to a low- and a high-phytate diet for growing pigs on the digestibilities of crude protein, amino acids, and energy. 1610 68

Phytase supplementation over a range of different levels of dietary Ca and nonphytate phosphorus (NPP) was investigated by comparing surface response curves from regression equations generated with (experiment 1) and without (experiment 2) phytase using various performance and bone quality parameters. Cobb x Cobb broiler chicks were raised from 0 to 16 d in 2 experiments using corn-soybean meal based diets. Experiment 1 used a 4 x 4 factorial arrangement with diets formulated to contain combinations of 4 levels of Ca: 0.38, 0.58, 0.78, and 0.98% and 4 levels of NPP: 0.2, 0.3, 0.4, and 0.5%. Experiment 2 used a composite rotatable design in which rations were formulated to contain dietary Ca levels of 0.38, 0.47, 0.68, 0.89, and 0.98% and NPP levels of 0.20, 0.24, 0.35, 0.46, and 0.50%. An extra point was included in the design to contain the lowest Ca and lowest NPP levels (0.38% Ca and 0.20% NPP). All combinations of Ca and NPP were fed with 657 phytase units/kg Natuphos 5000 phytase, plus 4 combinations (0.38% Ca and 0.20% NPP, 0.47% Ca and 0.24% NPP, 0.68% Ca and 0.35% NPP, and 0.89% Ca and 0.46% NPP) were fed without phytase to determine the suitability of comparing multiple regression response surfaces for particular variables among experiments. Comparison of surfaces, with and without phytase, showed that growth and bone quality responses to phytase were greatest at low NPP levels and high Ca levels, and these decreased when the Ca level was reduced or when the NPP level was increased. A third experiment confirmed that phytase elicits a greater response at higher Ca levels and lower NPP levels (0.86% Ca and 0.20% NPP) versus low Ca levels and low NPP levels (0.47% Ca and 0.24% NPP). The data demonstrated why it is impossible to determine a single NPP equivalency value for phytase supplements.
Poult Sci 2005 Sep
PMID:Effects of calcium and nonphytate phosphorus concentrations on phytase efficacy in broiler chicks. 1620 62

Two heterologous phytases from Aspergillus awamori and Aspergillus fumigatus obtained from submerged cultures of genetically modified fungal strains in addition to two commercially available phytase preparations (Allzyme and Natuphos phytases) were purified to homogeneity using a combination of ultrafiltration, gel filtration and ion exchange. The purified preparations were used in subsequent characterisation studies, in which Western Immunoblot analysis, pH and temperature optima, thermal stability and substrate specificity were assessed. A. fumigatus phyA phytase expressed in A. awamori exhibited activity over a broad pH range together with an increased temperature optimum, and slightly enhanced thermal stability compared to the other phytases tested, and is thus a promising candidate for animal feed applications. This particular phytase retains activity over a wide range of pH values characteristic of the digestive tract and could conceivably be more suited to the increasingly higher feed processing temperatures being utilised today, than the corresponding phytases from Aspergillus niger.
Bioresour Technol 2006 Sep
PMID:Purification and physico-chemical characterisation of genetically modified phytases expressed in Aspergillus awamori. 1624 22

The sequence in which a variety of enzymes and metabolites are affected by gibberellic acid after application of the hormone to aleurone layers of half seeds of barley (Hordeum vulgare var. Betzes) and half seeds of wheat (Triticum aestivum var. Gensee) was investigated. With barley aleurone layers the first hormonal effect observed was the increased secretion of soluble carbohydrate, some of which appears to be a glucan containing some beta-1,3 linkages. This was followed by increased oxygen consumption and increased secretion of ATPase, GTPase, phytase, phosphomonoesterase, phosphodiesterase, inorganic phosphate, carbohydrates other than amylase, peroxidase and amylase. Similar sequential effects were seen in wheat half seeds. Increased activity of alcohol dehydrogenase in barley seeds was elicited by the hormone but there was no effect on glucose-6-phosphate isomerase.
Plant Physiol 1969 Sep
PMID:A survey of the sequence of some effects of gibberellic Acid in the metabolism of cereal grains. 1665 95

A phytase was isolated and partially purified from the pollen of Lilium longiflorum Thumb. Optimum activity was at pH 8.0. The phytase was activated by Ca(2+) and Sr(2+) but not by the other divalent cations tested. Activity was inhibited by ethylenediaminetetraacetate. The phytase had a temperature optimum of 55 to 60 degrees C and an activation energy of about 12,700 calories/mole. Extraction of L. longiflorum pollen with 0.1% Triton X-100 increased recovery of the phytase by nearly 4-fold. The phytase had a molecular weight of about 88,000 as determined by gel filtration chromatography and a K(m) value of 7.2 micromolar for phytic acid in the presence of Ca(2+).
Plant Physiol 1986 Sep
PMID:A Calcium-Activated Phytase from Pollen of Lilium longiflorum. 1666 18

Phytic acid is the most abundant inositol phosphate in cells; it constitutes 1-5% of the dry weight of cereal grains and legumes. Phytases are the primary enzymes responsible for the hydrolysis of phytic acid and thus play important roles in inositol phosphate metabolism. A novel alkaline phytase in lily pollen (LlALP) was recently purified in our laboratory. In this paper, we describe the cloning and characterization of LlALP cDNA from lily pollen. Two isoforms of alkaline phytase cDNAs, LlAlp1 and LlAlp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, were identified. The deduced amino acid sequences contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, but shares < 25% identity to fungal histidine acid phytases. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%). mRNA corresponding to LlAlp1 and LlAlp2 were expressed in leaves, stem, petals and pollen grains. The expression profiles of LlAlp isoforms in anthers indicated that mRNA corresponding to both isoforms were present at all stages of flower development. The expression of LlAlp2 cDNA in Escherichia coli revealed the accumulation of the active enzyme in inclusion bodies and confirmed that the cDNA encodes an alkaline phytase. In summary, plant alkaline phytase is a member of the histidine phosphatase family that includes MINPP and exhibits properties distinct from bacterial and fungal phytases.
Phytochemistry 2006 Sep
PMID:Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP). 1686 Mar 50

This paper reports the surface activity of phytase at the air-water interface, its interaction with lipid monolayers, and the construction of a new phytic acid biosensor on the basis of the Langmuir-Blodgett (LB) technique. Phytase was inserted in the subphase solution of dipalmitoylphosphatidylglycerol (DPPG) Langmuir monolayers, and its incorporation to the air-water interface was monitored with surface pressure measurements. Phytase was able to incorporate into DPPG monolayers even at high surface pressures, ca. 30 mN/m, under controlled ionic strength, pH, and temperature. Mixed Langmuir monolayers of phytase and DPPG were characterized by surface pressure-area and surface potential-area isotherms, and the presence of the enzyme provided an expansion in the monolayers (when compared to the pure lipid at the interface). The enzyme incorporation also led to significant changes in the equilibrium surface compressibility (in-plane elasticity), especially in liquid-expanded and liquid-condensed regions. The dynamic surface elasticity for phytase-containing interfaces was investigated using harmonic oscillation and axisymmetric drop shape analysis. The insertion of the enzyme at DPPG monolayers caused an increase in the dynamic surface elasticity at 30 mN m(-)(1), indicating a strong interaction between the enzyme and lipid molecules at a high-surface packing. Langmuir-Blodgett (LB) films containing 35 layers of mixed phytase-DPPG were characterized by ultraviolet-visible and fluorescence spectroscopy and crystal quartz microbalance nanogravimetry. The ability in detecting phytic acid was studied with voltammetric measurements.
Langmuir 2006 Sep 26
PMID:Fabrication of phytic acid sensor based on mixed phytase-lipid Langmuir-Blodgett films. 1698 69

For biochemical modification of the root-soil interface, the engineered secretion of stable enzymes from trichoblasts (= root hair bearing rhizodermal cells) is proposed. As a reporter activity, we chose to express a synthetic gene encoding a secretory phytase (PHY) directed by a trichoblast-specific promoter in root hair cells of the crop plant potato. Transgenic plants produced and secreted phytase in sufficient amounts to release phosphate from phytate in liquid medium. When grown in an unsterile substrate containing phytate, transgenic plants accumulated 40% more P in leaves than wild-type plants. The improved P nutrition driven by trichoblast-targeted expression and subsequent secretion of PHY illustrates the potential of using trichoblast-targeted expression of suitable enzymes for future applications in plant nutrition, phytoremediation and molecular farming.
Plant Biotechnol J 2003 Sep
PMID:Engineering the root-soil interface via targeted expression of a synthetic phytase gene in trichoblasts. 1716 34


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