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 rapid purification scheme utilizing three chromatographic steps resulted in 6 fold purification of Aspergillus ficuum phytase (myo-inositol-hexakisphosphate 3-phosphohydrolase, EC 3.1.3.8). At pH 5.0 and 60 degrees C the enzyme performed acceptably for 2.0 hr with only 30% diminished catalytic rate at the end. Substrate concentration exceeding 2mM was inhibitory. The inorganic orthophosphate, the product and a weak inhibitor, exhibited a Ki of 1.9 x 10(-3)M. The extracellular phytase has the potential for industrial use since it can be over produced, easily purified, remain catalytically active for a longer period and is not subjected to severe product inhibition.
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PMID:Production, rapid purification and catalytic characterization of extracellular phytase from Aspergillus ficuum. 285 6

Purified Aspergillus ficuum phytase's partial primary structure and amino acid and sugar composition were elucidated. Determination of kinetic parameters of the enzyme at different pH values and temperatures indicated no significant alteration of the Km for phytate while the Kcat was affected. The enzyme was able to release more than 51% of the total available Pi from phytate in a 3.0 hr assay at 58 degrees C, but the Kcat dropped to 15% of the initial rate. Substrate selectivity studies revealed phytate to be the preferred substrate. The pH optima of phytase was 5.0, 4.0, and 3.0 for phytate, ATP, and polyphosphate, respectively. The enzyme had varied sensitivity towards cations. While Ca++ and Fe++ produced no effect on the catalytic rate of the enzyme, Cu+, Cu++, Zn++, and Fe were found to be inhibitory. Mn++ was observed to enhance enzyme activity by 33% at 50 microM. Known inhibitors of acid phosphatases e.g. L (+)-tartrate, phosphomycin, and sodium fluoride had no effect on enzyme activity.
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PMID:Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. 285 7

Aspergillus ficuum phytase was covalently immobilized on Fractogel TSK HW-75 containing 2-oxy-l-alkylpyridinium salts. A packed-bed bioreactor was constructed with the immobilized phytase. An HPLC ion-exchange method was used to analyze the enzymatic products of the bioreactor. Immobilized fungal phytase was able to hydrolyze myo-inositol Hexa-, penta-, tetra-, tri-, and diphosphates. When the substrate solution was recirculated for 5 hr in the bioreactor about 50% inorganic orthophosphate was released and myo-inositol-diphosphate and mono-phosphate were the only remaining products.
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PMID:Immobilization of Aspergillus ficuum phytase: product characterization of the bioreactor. 285 8

Rhizopus oligosporus strain CT11K2, commonly used in tempeh (fermented soybean) production produced both extra- and intracellular phytases. The enzymes were isolated from growth media and the cultured mould and partially purified by acetone fractionation, gel filtration on Sephadex G-100 and DEAE-cellulose chromatography. Intracellular phytase activity was higher than that of the extracellular enzyme. Both enzymes showed maximum activity at pH 4.5 and 55 degrees C, suggesting relatively high thermostability. The enzymes were partially inhibited by high concentrations of substrate. The Km and Vmax values of the extracellular phytase were 0.15 mM and 0.076 mumol Pi per min per ml DEAE-cellulose purified enzyme, respectively, and for the intracellular phytase were 0.17 mM and 0.34 mumol Pi per min per ml enzyme, respectively. Extracellular phytases showed inactivation and activation energies for the hydrolysis of phytic acid of approximately 28,300 cal per mol and 6100 cal per mol, respectively, while inactivation and activation energies for the intracellular phytase were approximately 33,200 per mol and 9500 cal per mol, respectively.
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PMID:Characterization of extra- and intracellular phytases from Rhizopus oligosporus used in tempeh production. 285 46

The activity and basic kinetic constants of phytase were studied in chicken erythrocytes during animal development. The regulatory inhibition of phytase by IHP and 2,3-BPG takes place at key stages of the development. As in mammals, there is a specific control of the levels of organic phosphate involved in the oxygenation process of haemoglobin, during animal development.
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PMID:Phytase activity in chicken erythrocytes and its control by organic phosphates (glycerate-2,3-P2 and inositol-P5) during avian development. 298 56

Alkaline phosphatase, highly purified from bovine intestinal mucosa, has significant hydrolytic activity against phytate and CaATP. Phytase and CaATPase activities require quite different assay conditions than those which are optimal for conventional alkaline phosphatase substrates such as 4-nitrophenyl phosphate. We have used affinity chromatography and antibody recognition to demonstrate that the phytase and CaATPase activities are not due to contaminating enzymes, but are intrinsic activities of intestinal alkaline phosphatase. All of the phytase and CaATPase activities present in crude extracts of bovine intestinal mucosa can be accounted for by alkaline phosphatase. Apparently neither phytase nor CaATPase exist in this tissue as independent enzymes. Specific substrates which require assay conditions quite different from the conventional 4-nitrophenyl phosphate substrate may account for the physiological function of "alkaline phosphatase."
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PMID:The relationship of alkaline phosphatase, CaATPase, and phytase. 299 87

Two separate balance experiments of P, Ca, Mg and Zn were carried out on 5 lots of 4 growing pigs each (35-40 kg) adapted for 3 weeks to one of the diets studied. In the first experiment, the control diet was compared with a diet containing 20% of coarse wheat bran, thus richer in minerals, the quantities ingested not being equalized. In the second experiment, three diets were compared: a control diet, a diet with 2.5% of high-methoxylated (HM) apple pectin, and a diet with 2.5% low-methoxylated (LM) apple pectin. The supplement of P and Mg provided by the wheat bran was well absorbed (apparent absorption) and retained by the pigs. On the contrary, in spite of higher intake of Ca and Zn with bran diet, the absorption of these minerals was not improved. The action of wheat bran phytase and the possible absorption of P and Mg (but not of Ca and Zn) in the large intestine could explain these results. Compared to HM pectin that had relatively little effect on mineral utilization, LM pectin drastically diminished the absorption and retention of the minerals studied and resulted in negative Ca, Mg and Zn balances. The degree of pectin esterification would thus be the main factor determining the effect of pectin on mineral availability. In conclusion, wheat bran is a source of available P and Mg for the pig but it might have an unfavorable effect on the utilization of Ca and Zn. LM pectin produces a deleterious influence on mineral balances.
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PMID:Effect of wheat bran and pectin on the absorption and retention of phosphorus, calcium, magnesium and zinc by the growing pig. 299 94

At least two-thirds of the phosphorus ingested by pigs is in the form of phytates. Two intestinal vitamin D-sensitive enzymes, alkaline phosphatase and phytase, might be involved in phytate-P digestion. The effects of dietary vitamin D upon the two intestinal phosphatases and P utilization in pigs fed a high phytate-P diet are reported here. Fourteen vit. D-depleted pigs (25-hydroxy vit. D: about 2 ng/ml plasma) were divided into two groups fed the same basal diet containing 0.6% P (of which 80% was phytic) and 0.6% Ca. One group (+D) was supplemented for 5 weeks with vit. D (1 000 IU D3/kg diet) and the other (-D) received none. P absorption and retention was two times higher in +D pigs than in -D animals (balance technique), and tibia X-ray pictures showed a lower bone density with the -D diet than with the +D diet. Surprisingly, vit. D supplementation had no effect on either of the mucosal enzymes (phytase and alkaline phosphatase). It may be concluded that vit. D improves phytate-P absorption via a mechanism which does not involve an increase in the activity of the intestinal phosphatases.
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PMID:[Absence of effect of vitamin D on intestinal phytase and alkaline phosphatase: relation with phytic phosphorus in the pig]. 299 95

The possibility that inositolphosphatase differs from other intestinal phosphatases was tested by comparing several enzymatic characteristics of phosphatase activities of rat intestinal homogenate acting on various specific substrates. Optimum pH and temperature, Km, Vmax, heat stability, inhibition and metal ion requirement studies suggest that inositolphosphatase differs from phytase and p-nitrophenylphosphatase. Furthermore, we found that inositolphosphatase activity was about 2 times higher in duodenum and jejunum than ileum. It sedimented (90-100%) with a high-speed particulate fraction of mucosal homogenate; 42% of the activity was separated with the brush border membrane isolated from mucosal homogenate. Partial separation by gel filtration on Sephadex G200 and chromatography on phenyl Sepharose CL 4B provided additional evidence to suggest that inositolphosphatase and phytase are different enzymes.
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PMID:Studies on inositolphosphatase in rat small intestine. 299 53

Phytic acid in food is considered to be responsible for a reduced bioavailability of essential dietary minerals; its detrimental effects can be diminished by hydrolysis with phytase during processing. The average phytic acid content was 8.18 mg/g and 3.44 mg/g and average phytase activity was 3.7 U/g and 2.6 U/g in rye kernels and in flour (Type 997, 1.09 ash content), respectively. Phytate and Phytase were about equally distributed between the two kernel halves (cross sections). During the early stages of germination (3 days) phytase activity did not change, and phytic acid content was reduced to 67%. After milling most of the phytic acid and phytase activity were found in the bran fractions. It is concluded that substrate and enzyme are present in the same kernel structures but separate within the cells. Cooking of ground rye caused a phytate hydrolysis which was the more effective 1.) the smaller the particle sizes were, 2.) the more water was added, and 3.) the longer phytase worked at optimum temperature. Extrusion cooking of the rye whole flour at up to 100 degrees C did not influence the phytic acid level but caused a 23% reduction at 170 degrees C. Phytase activity was reduced by 80% by extrusion cooking at 80 degrees C.
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PMID:[Phytic acid and cereals and cereal products. I: Phytic acid and phytase in rye and rye products]. 301 3


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