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)

An enzyme which liberates Pi from myo-inositol hexaphosphate (phytic acid) was shown to be present in culture filtrates of Bacillus subtilis. It was purified until it was homogeneous by ultracentrifugation, but it still showed two isozymes on polyacrylamide gel electrophoresis. The enzyme differed from other previously known phytases in its metal requirement and in its specificity for phytate. It had a specific requirement for Ca2+ for its activity. The enzyme hydrolyzed only phytate and had no action on other phosphate esters tested. This B. subtilis phytase is the only known phytate-specific phosphatase. The products of hydrolysis of phytate by this enzyme were Pi and myo-inositol monophosphate. The enzyme showed optimum activity at pH 7.5. It was inhibited by Ba2+, Sr2+, Hg2+, Cd2+, and borate. Its activity was unaffected by urea, diisopropylfluorophosphate, arsenate, fluoride, mercaptoethanol, trypsin, papain, and elastase.
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PMID:Purification and properties of phytate-specific phosphatase from Bacillus subtilis. 628 90

The phyA gene encoding an extracellular phytase from the thermophilic fungus Thermomyces lanuginosus was cloned and heterologously expressed, and the recombinant gene product was biochemically characterized. The phyA gene encodes a primary translation product (PhyA) of 475 amino acids (aa) which includes a putative signal peptide (23 aa) and propeptide (10 aa). The deduced amino acid sequence of PhyA has limited sequence identity (ca. 47%) with Aspergillus niger phytase. The phyA gene was inserted into an expression vector under transcriptional control of the Fusarium oxysporum trypsin gene promoter and used to transform a Fusarium venenatum recipient strain. The secreted recombinant phytase protein was enzymatically active between pHs 3 and 7.5, with a specific activity of 110 micromol of inorganic phosphate released per min per mg of protein at pH 6 and 37 degrees C. The Thermomyces phytase retained activity at assay temperatures up to 75 degrees C and demonstrated superior catalytic efficiency to any known fungal phytase at 65 degrees C (the temperature optimum). Comparison of this new Thermomyces catalyst with the well-known Aspergillus niger phytase reveals other favorable properties for the enzyme derived from the thermophilic gene donor, including catalytic activity over an expanded pH range.
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PMID:Molecular characterization and expression of a phytase gene from the thermophilic fungus Thermomyces lanuginosus. 979 1

1. Ducklings were given diets with vegetable protein (VP) and 0 or 600 g rice bran/kg; fish meal (60 g/kg) and a phytase (+, -) were added to the diets (VP + AP). An additional 40 g soyabean meal/kg was added to the diet with rice bran (VP ++). Amino acid digestibility and mineral retention were measured in the lower ileum of ducklings killed at 23 d of age. Acid insoluble ash was used as an inert marker. Trypsin and amylase activities were also measured and weights of the pancreas and small intestine recorded at slaughter. 2. Addition of soyabean meal (VP ++) to the diet with rice bran improved growth rate and food intake compared to the diet without (VP) and gave the same food intake and growth rate as the comparable basal diet (VP) without rice bran. Fish meal improved growth rate on the diets without rice bran and improved food intake on this diet (VP + AP). Rice bran depressed growth rate and food conversion ratio (FCR); protein source affected growth rate, food intake and FCR; phytase increased food intake only. There were several interactions. 3. Determined total amino acid composition of the diets appeared to meet the essential amino acid requirements of ducklings. Rice bran depressed the ileal digestibility of virtually all amino acids and phytase had no direct effect, although there were interactions. Fish meal addition to diets with rice bran improved the apparent digestibility of several essential amino acids as well as that of dry matter and crude protein. 4. Ileal retention of some minerals and tibia ash content were reduced by rice bran. Fish meal and phytase inclusion increased P retention and ash in tibia. 5. Higher intestinal trypsin activity and increased pancreas size were seen in ducklings on diets with rice bran compared to those without. Intestinal amylase activity was reduced in ducklings given rice bran, probably because of its low starch content. 6. The stimulating effect of fish meal on duckling performance was probably caused in part by the improvement in the digestibility of some amino acids. The addition of small amounts of minerals in fish meal may have increased mineral retention. Phytase gave benefits anticipated from our previous work, but also improved lysine and threonine digestibility in diets containing vegetable protein only.
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PMID:Strategies to improve the nutritive value of rice bran in poultry diets. IV. Effects of addition of fish meal and a microbial phytase to duckling diets on bird performance and amino acid digestibility. 992 13

Proteolysis of two purified recombinant enzymes, namely, the Aspergillus niger phytase (r-PhyA) and the Escherichia coli pH 2.5 acid phosphatase (r-AppA), by pepsin and trypsin was investigated in this study. After r-PhyA and r-AppA were incubated with different concentrations of pepsin or trypsin, their residual phytase activities and amounts of inorganic phosphorus released from soybean meal were determined. Both enzymes retained more than 85% of their original activities at the trypsin/phytase ratios (w/w) 0.001 and 0. 005, while r-AppA and r-PhyA lost 60 and 20% of the original activity at the ratio of 0.01 or 0.025, respectively. In contrast, there was a 30% increase in phytase activity after r-AppA was incubated with pepsin at the ratios of 0.005 or 0.01. Meanwhile, r-PhyA lost 58 to 77% of its original activity under the same conditions. Trypsin and pepsin affected the hydrolysis of phytate phosphorus from soybean meal by r-AppA and r-PhyA in a similar way to their residual phytase activities. All of these in vitro proteolyses were confirmed by SDS-PAGE analysis. Our results demonstrate different sensitivities of r-AppA and r-PhyA to trypsin and pepsin, suggesting active trypsin resistant r-PhyA and pepsin resistant r-AppA polypeptides.
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PMID:Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro. 1032 21

Aspergillus fumigatus phytase is a heat-stable enzyme of great potential. Our objective was to determine if a high level of functional expression of the A. fumigatus phytase gene could be produced in Pichia pastoris and how the recombinant phytase reacted to different substrates, heating conditions, and proteases. A 1.4-kb DNA fragment containing the coding region of the gene was inserted into the expression vector pPICZalphaA and expressed in P. pastoris as an active, extracellular phytase (r-Afp). The yield was 729 mg of purified protein per liter of culture, with a specific activity of 43 units/mg of protein. The enzyme r-Afp shared similar pH and temperature optima, molecular size, glycosylation extent, and specificity for p-nitrophenyl phosphate and sodium phytate to those of the same enzyme expressed in A. niger. Given 20 min of exposure to 65 to 90 degrees C, the enzyme retained 20 to 39% higher residual activity in 10 and 200 mM sodium acetate than that in sodium citrate. The enzyme seemed to be resistant to pepsin digestion, but was degraded by high levels of trypsin. In conclusion, P. pastoris is a potential host to express high levels of A. fumigatus phytase and the thermostability of the recombinant enzyme is modulated by the specificity of buffer used in the heat treatment.
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PMID:Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme. 1067 11

The effect of mild hydrothermal treatment and the addition of phytase under optimal conditions (pH 5.5, 37 degrees C) on the nutritive utilization of the protein of pea (Pisum sativum L.) flour was studied in growing rats by examining the chemical and biological balance. Mild hydrothermal treatment produced reductions of 83, 78, and 72%, respectively, in the levels of alpha-galactosides, phytic acid, and trypsin inhibitors and also produced a significant increase in the digestive utilization of protein. The additional fall in the levels of phytic acid caused by the addition of phytase did not lead to a subsequent improvement in the digestive utilization of protein. The mild hydrothermal treatment of pea flour produced a significant increase in the metabolic utilization of protein and carbohydrates, which was reflected in the protein efficiency ratio and food transformation growth indices. These effects were not observed in the phytase-supplemented pea diet.
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PMID:Nutritional evaluation of pea (Pisum sativum L.) protein diets after mild hydrothermal treatment and with and without added phytase. 1267 Jan 90

Citrobacter braakii YH-15 produced an intracellular phytase which was purified 12800 fold to homogeneity with the specific activity of 3457 units mg(-1), which is 1.9 times higher than E. coli phytase previously recorded as having the highest specific activity. Its molecular weight was 47 kDa by SDS-PAGE gel. Enzyme activity was optimal at pH 4 and at 50 degrees C. The Km value for sodium phytate was 0.46 mM with a Vmax 6027 U mg(-1). The phytase was resistant to proteases such as trypsin, pepsin, papain, pancreatin, and elastase.
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PMID:Isolation and characterization of a phytase with improved properties from Citrobacter braakii. 1451 72

Digestibility of protein in traditional diets from developing countries such as India, Guatemala, and Brazil is considerably lower compared to that of protein in typical North American diets (54-78 versus 88-94%). The presence of less digestible protein fractions, high levels of insoluble fiber, and high concentrations of antinutritional factors in the diets of developing countries, which are based on less refined cereals and grain legumes as major sources of protein, are responsible for poor digestibility of protein. The effects of the presence of some of the important antinutritional factors on protein and amino digestibilities of food and feed products are reviewed in this chapter. Food and feed products may contain a number of antinutritional factors that may adversely affect protein digestibility and amino acid availability. Antinutritional factors may occur naturally, such as glucosinolates in mustard and rapeseed protein products, trypsin inhibitors and hemagglutinins in legumes, tannins in legumes and cereals, phytates in cereals and oilseeds, and gossypol in cottonseed protein products. Antinutritional factors may also be formed during heat/alkaline processing of protein products, yielding Maillard compounds, oxidized forms of sulfur amino acids, D-amino acids, and lysinoalanine (LAL, an unnatural amino acid derivative). The presence of high levels of dietary trypsin inhibitors from soybeans, kidney beans, or other grain legumes can cause substantial reductions in protein and amino acid digestibilities (up to 50%) in rats and pigs. Similarly, the presence of high levels of tannins in cereals, such as sorghum, and grain legumes, such as fababean (Vicia faba L.), can result in significantly reduced protein and amino acid digestibilities (up to 23%) in rats, poultry, and pigs. Studies involving phytase supplementation of production rations for swine or poultry have provided indirect evidence that normally encountered levels of phytates in cereals and legumes can reduce protein and amino acid digestibilities by up to 10%. D-amino acids and LAL formed during alkaline/heat treatment of proteins such as casein, lactalbumin, soy protein isolate, or wheat proteins are poorly digestible (less than 40%), and their presence can reduce protein digestibility by up to 28% in rats and pigs. A comparison of the protein digestibility determination in young (5-week) versus old (20-month) rats suggests greater susceptibility to the adverse effects of antinutritional factors in old rats than in young rats. Therefore, the inclusion of protein digestibility data obtained with young rats, as the recommended animal model, in the calculation of PDCAAS (Protein Digestibility-Corrected Amino Acid Score) may overestimate protein digestibility and quality of products, especially those containing antinutritional factors, for the elderly. For products specifically intended for the elderly, protein digestibility should be determined using more mature rats.
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PMID:Effects of antinutritional factors on protein digestibility and amino acid availability in foods. 1600 74

Phytase (myo-inositol-1,2,3,4,5,6-hexakisphosphate phosphohydrolase, EC 3.1.3.26) catalyses the stepwise hydrolysis of phytic acid (myo-inositol hexakisphosphate). Phytases are of great commercial importance due to their usage as supplement of food and animal feed, which can cater to nutrition demands and alleviate environmental problems, has been approved by many countries. Although acid phytases have been extensively studied, information regarding the phytases from Citrobacter is limited. In the work presented, a phytase was separated from Citrobacter freundii. After steps of electrophoretic homogeneity by successive ammonium sulfate between 60% and 80% saturation precipitation, DEAE-Sepharose ion-exchange chromatography and gel filtration through Superdex HR 10/30, final gel elution resulted in a 41.3-fold purification and yield of 9.3%. Gel elution is an effective method to purify the protein which contaminated with a few other proteins. The purified preparations were used in subsequent characterization studies. Based on SDS-PAGE analysis, the molecular weight of the purified phytase was calculated to be approximately 45.0kDa in monomeric form. The pure enzyme has an optimum pH of 4.0 to approximately 4.5. It was found stable between pH5.0 to approximately 7.0, about 90% of the enzyme activity was retained at 37 degrees C for 60min. The phytase has an optimum temperature of 40 degrees C which was lower than that of other phytases from Aspergillus or E. coli (average 50 to approximately 60 degrees C) and was close to the temperature of gastrointestinal tract in animals (37 to approximately 40 degrees C). Thus the enzyme is a promising candidate for animal feed applications. Activity of the purified phytase was influenced by changing the reaction temperature. Data showed that the enzyme retained its activity over a long period when stored at 4 degrees C, whereas thermal inactivation studies indicated that the enzyme lost 100% activity after treatment at 60 degrees C for 4min. The Km values of the phytase for dodecasodium phytate at 37 degrees C was 0.85nmol/L with a Vmax 0.53IU/(mg x min). Phytase activity was strongly inhibited by SDS, Zn2+ and moderately inhibited by Cu2+, Cr3+, Fe2+ and Fe3+. Activity was not significantly affected by EDTA, K+, Mg2+ and Ca2+. The phytase has excellent resistance to trypsin, but not pepsin. The N-terminal amino acids sequence of the phytase protein was determined as QCAPEGYQLQQVLMM which exhibited about 80% homology to Glucose-1-phosphatases from E. coli, Shigella flexneri and Salmonella, whereas it did not show apparent sequence similarity with any other phytase listed in the databases. Initial characterization of the purified enzyme suggested that it is a potential candidate for use as an animal feed supplement.
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PMID:[Purification and properties of Citrobacter freundii phytase]. 1657 82

A Yersinia intermedia strain producing phytase was isolated from glacier soil. The phytase gene, appA, was isolated by degenerate PCR and TAIL-PCR. The full-length fragment contained 2354bp with a 1326-bp open reading frame encoding 441 amino acids. APPA contained the active site RHGXRXP and HD sequence motifs that are typical of histidine acid phosphatases. To our knowledge, this is the first report of the detection of phytase activity and cloning of the relevant gene from Y. intermedia. The gene was overexpressed in Pichia pastoris, and the purified recombinant APPA had a specific activity for sodium phytate of 3960U/mg, which is higher than that of the Citrobacter braakii phytase (previously the highest specific activity known). Recombinant APPA had high activity from pH 2 to 6 (optimum 4.5) and optimal temperature of 55 degrees C; the enzyme was resistant to pepsin and trypsin. These characteristics suggest that APPA may be highly suitable for use in the feed industry.
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PMID:A novel phytase with preferable characteristics from Yersinia intermedia. 1703 58


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