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)

Of all the sources of phytase that have been studied (plant, animal, and microorganisms), the highest yields are produced by a wild-type strain A. niger NRRL 3135 (12.7 mg P/hr/ml = 6.8 microns P/ml/min = 113.9 nKat/ml) in a mineral salt medium in which total phosphate (4 mg %) is limiting for growth and cornstarch and glucose are the carbon sources. Synthesis of the enzyme is repressed by phosphate in the wild-type strain. Aspergillus niger NRRL 3135 produces two phytases one with pH optima at 2.5 and 5.5 (phyA) and one with an optimum at pH 2.0 (phyB). It also produces a pH 6.0 optimum phosphatase that has no phytase activity. These three glycoproteins have been purified to homogeneity, characterized, sequenced, and cloned. The sequences have been compared to each other, other phytases, and to known phosphatases. Their homology has been determined. The active sites of phytases show remarkable homology to the active site residues of the members of a particular class of acid phosphatase (histidine phosphatase). The most conserved sequence is RHGXRXP. Phytase has been covalently immobilized on Fractogel TSK HW-75 F and glutaraldehyde-activated silicate. It has been immobilized on agarose. Losses of activity have been noted on immobilization but these may be minimized by future research. It should be possible to commercially produce and recover penta-, tetra-, tri-, di-, and monoinositol phosphates using immobilized phytase if markets develop for those products. Phytase (phyA) from A. niger NRRL 3135 has been cloned into an A. niger glucoamylase producing strain CBS 513.88 using a construct that has a glucoamylae promoter and an A. niger NRRL 3135 leader sequence, and that is devoid of phosphate repression. The yield of the secreted enzyme was increased 52-fold above that of wild-type A. niger NRRL 3135. The bioengineered organism produces 270 microns P/ml/min (4500 nKat/ml) which is approximately 7.9 g/liter in the medium. The yield of the secreted enzyme was increased 1440-fold above that of wild type CBS 513.88. Commercial preparations of the cloned enzyme are available. Phytase (phyA) has been cloned into tobacco and canola. The enzyme is localized in the seed and expressed at high levels. Feeding of the seed to animals has made the phytin-P in the commercial diets available to the animals. The efficacy of feeding phytase to monogastric animals (poultry and swine) has been established. The amount of enzyme that is necessary to be added to commercial diets has been titred for broilers, layers, turkeys, ducks, and swine. The units of enzyme required are related to the phytin-P content in the diet. The use of the enzyme as a feed additive has been cleared in 22 countries. If phytase were used in the diets of all of the monogastric animals reared in the U.S., it would release phosphorus that has a value of $1.68 x 10(8) per year. The FDA has approved the enzyme preparation as GRAS. The effect of feeding phytase to animals enables assimilation of the P found in feed ingredients and diminishes the amount of phosphate in the manure and subsequently entering the environment. The effect of feeding phytase to animals on pollution has been quantitatively determined. If phytase were used in the diets of all of the monogastric animals reared in the United States, it would preclude 8.23 x 10(7) kg P from entering the environment.
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PMID:Phytase. 886 87

In the nutrition of monogastric animals phytate-P represents a poorly available source of phosphorus, especially in the case of diets low in phytase activity. Similarly the bioavailability of different minerals and trace elements is considerably reduced by phytate complexes. High concentrations of Ca increase the anti-nutritive effect of phytic acid on mineral and trace element bioavailability and thus impede the action of phytase. This effect can in part be compensated by an increased supply of vitamin D. There is also evidence for protective functions of phytic acid such as the prevention of the formation of free radicals, the delaying of post prandial glucose absorption, the decrease in plasma cholesterol and triglycerides as well as a change in the carry over of heavy metals. The basic mechanisms by which phytic acid may exert these effects are still not clear. In several studies reported in the literature, evidence for the nutritional significance and ecological importance of microbial phytase for pigs and poultry has been given. As the monogastric organism contains no or only negligible amounts of endogenous phytase in the stomach and small intestine, it is therefore dependent on plant or microbial phytase. Plant phytase, e.g. from rye, triticale, wheat or, in smaller amounts from barley, and supplemented Aspergillus-phytase display cumulative effects.
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PMID:Nutritional significance of phytic acid and phytase. 934 95

An efficient process was developed for the low-cost production of phytases using Hansenula polymorpha. Glucose or glucose syrups, previously reported as repressive substrates, were used as main carbon sources during fermentation. Glucose was even the most productive substrate for high-level production of phytases. Compared with the process using glycerol, the standard carbon source used for this process until now, the use of glucose led to a reduction of more than 80% in the raw materials costs. In addition, exceptionally high concentrations of active enzyme (up to 13.5 g/L) were obtained in the medium, with phytase representing over 97% of the total accumulated protein. These levels greatly exceed those reported so far for any yeast-based expression system. Very efficient downstream processing procedures were developed with product recovery yields over 90%. Both the fermentation and downstream processing were successfully tested in pilot scale up to 2000 L. As a result, H. polymorpha can be used as a highly competitive system for low-cost phytase production.
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PMID:An expression system matures: a highly efficient and cost-effective process for phytase production by recombinant strains of Hansenula polymorpha. 1009 17

Phytases hydrolyze myo-inositol 1,2,3,4,5,6-hexaphosphate (IP(6)), yielding lower inositol phosphates and inorganic orthophosphate. Two commercial strains of baker's yeast (Saccharomyces cerevisiae), Y(1) and Y(2), were able to express phytase activity. This was determined by the capacity to grow in a synthetic medium with IP(6) as the sole phosphorus source. IP(6) hydrolysis was rapid for both strains, and after 24 h, all IP(6) was degraded. Control cultures contained inorganic orthophosphate (P(i)) and no IP(6). Growth rate in IP(6) medium was for both strains essentially identical to growth in P(i) medium, indicating a well-adapted metabolism for utilization of phosphorus from IP(6). There was some difference in growth yield (milligrams of biomass per milligram of glucose) between the two strains: 0.95 (Y(1)) and 1.35 (Y(2)) in IP(6) medium and 1.03 and 1. 35, respectively, in P(i) medium. The phytases were of the 3-phytase type, forming mainly DL-Ins(1,2,4,5,6)P(5), DL-Ins(1,2,5,6)P(4), and DL-Ins(1,2,6)P(3).
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PMID:Inositol hexaphosphate hydrolysis by Baker's yeast. Capacity, kinetics, and degradation products. 1063 59

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.
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PMID:Regulation of Raoultella terrigena comb.nov. phytase expression. 1188 66

Five strains of phytase-producing, gram-negative, non-spore-forming, non-motile, small, stout, rod-shaped, strictly anaerobic, fermentative bacteria were isolated from the rumens of cattle in Malaysia. All five strains had morphological, physiological and biochemical features in common. Although these strains had many physiological and biochemical characteristics that were identical to those of the Mitsuokella multacida type strain (ATCC 27723T), they could be distinguished from this species by means of the following characteristics: a smaller cell size (1.2-2.4 microm long and 0.6-0.8 microm wide); a lower final pH value (3.8-4.0) in peptone/yeast extract/glucose broth; inhibition by 0.001% brilliant green; insensitivity to kanamycin (100 microg ml(-1)) and penicillin (10 microg ml(-1)); a higher optimum growth temperature (approx. 42 degrees C); the ability to grow at 45 and 47 degrees C; the ability to ferment glycerol, sorbitol and amidon; and the inability to ferment mannitol, rhamnose, D-tagatose and melezitose. The G+C content of the type strain (M 9T) of these five strains was 56.9 mol%. Analysis of the 16S rRNA gene sequence of type strain M 9T indicated that the strain falls within the genus Mitsuokella. The sequence similarity between type strain M 9T and Mitsuokella multacida was 98.7%. The DNA-DNA relatedness between type strain M 9T and Mitsuokella multacida type strain DSM 20544T (= ATCC 27723T) was 63.8%, indicating that, in spite of a high level of similarity for the 16S rRNA gene sequence, type strain M 9T is independent of Mitsuokella multacida at the species level. On the basis of these results, a new species, Mitsuokella jalaludinii sp. nov., is proposed for these strains. The type strain is M 9T (= DSM 13811T = ATCC BAA-307T).
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PMID:Mitsuokella jalaludinii sp. nov., from the rumens of cattle in Malaysia. 1205 30

A bacterial strain capable of producing a thermo-acido-tolerant phytase was isolated from soil around haystacks and designated as strain PH01. The phytase produced was purified to homogeneity as determined by native PAGE. From SDS-PAGE, it was 30 kDa in size. The purified phytase was a thermo-acido-tolerant enzyme. A complex medium for the PH01 phytase production was developed. The medium, "PheB", was composed of 2% glucose, 0.2% CaCl(2), 0.5% NH(4)NO(3), 0.05% KCl, 0.05% MgSO(4).7H(2)O, 0.001% FeSO(4).7H(2)O, 0.001% MnSO(4).H(2)O in rice bran plus soybean meal extract containing 3% (v/v) phosphate solution (7.3% NaHPO(4)+3.2%KH(2)PO(4), pH 7.2). Cultivation was done at 37 degrees C with aeration for 48 h which produced phytase at 10 U/ml. Exposure of the phytase to 1% bile salt; i.e., taurocholate or deoxycholate, caused less than 15% reduction of activity. Potential application of PH01 phytase as a feed supplement was suggested.
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PMID:Thermo-acido-tolerant phytase production from a soil bacterium in a medium containing rice bran and soybean meal extract. 1250 70

Phytase production was studied by three Mucor and eight Rhizopus strains by solid-state fermentation (SSF) on three commonly used natural feed ingredients (canola meal, coconut oil cake, wheat bran). Mucor racemosus NRRL 1994 (ATCC 46129) gave the highest yield (14.5 IU/g dry matter phytase activity) on coconut oil cake. Optimizing the supplementation of coconut oil cake with glucose, casein and (NH(4))(2)SO(4), phytase production in solid-state fermentation was increased to 26 IU/g dry matter (DM). Optimization was carried out by Plackett-Burman and central composite experimental designs. Using the optimized medium phytase, alpha-amylase and lipase production of Mucor racemosus NRRL 1994 was compared in solid-state fermentation and in shake flask (SF) fermentation. SSF yielded higher phytase activity than did SF based on mass of initial substrate. Because this particular isolate is a food-grade fungus that has been used for sufu fermentation in China, the whole SSF material (crude enzyme, in situ enzyme) may be used directly in animal feed rations with enhanced cost efficiency.
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PMID:Production of phytase by Mucor racemosus in solid-state fermentation. 1267 65

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.
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PMID:Optimization of the extracellular production of a bacterial phytase with Escherichia coli by using different fed-batch fermentation strategies. 1276 60

Two experiments were conducted to determine the effect of phytase on energy availability in pigs. In Exp. 1, barrows (initial and final BW of 26 and 52 kg) were allotted to four treatments in a 2 x 2 factorial arrangement. Corn-soybean meal (C-SBM) diets were fed at two energy levels (2.9 and 3.2 x maintenance [M]) with and without the addition of 500 phytase units/kg of diet. The diets contained 115% of the requirement for Ca, available P (aP), and total lysine, and Ca and aP were decreased by 0.10% in diets with added phytase. Pigs were penned individually and fed daily at 0600 and 1700, and water was available constantly. Eight pigs were killed and ground to determine initial body composition. At the end of Exp. 1, all 48 pigs were killed for determination of carcass traits and protein and fat content by total-body electrical conductivity (TOBEC) analysis. Six pigs per treatment were ground for chemical composition. In Exp. 2, 64 barrows and gilts (initial and final BW of 23 and 47 kg) were allotted to two treatments (C-SBM with 10% defatted rice bran or that diet with reduced Ca and aP and 500 phytase units/kg of diet), with five replicate pens of barrows and three replicate pens of gilts (four pigs per pen). In Exp. 1, ADG was increased (P < 0.01) in pigs fed at 3.2 x M. Based on chemical analyses, fat deposition, kilograms of fat, retained energy (RE) in the carcass and in the carcass + viscera, fat deposition in the organs, and kilograms of protein in the carcass were increased (P < 0.10) in pigs fed the diets at 3.2 vs. 2.9 x M. Based on TOBEC analysis, fat deposition, percentage of fat increase, and RE were increased (P < 0.09) in pigs fed at 3.2 x M. Plasma urea N concentrations were increased in pigs fed at 3.2 x M with no added phytase but were not affected when phytase was added to the diet (phytase x energy, P < 0.06). Fasting plasma glucose measured on d 28, ultrasound longissimus muscle area (LMA), and 10th-rib fat depth were increased (P < 0.08) in pigs fed phytase, but many other response variables were numerically affected by phytase addition. In Exp. 2, phytase had no effect (P > 0.10) on ADG, ADFI, gain:feed, LMA, or 10th-rib fat depth. These results suggest that phytase had small, mostly nonsignificant effects on energy availability in diets for growing pigs; however, given that phytase increased most of the response variables measured, further research on its possible effects on energy availability seems warranted.
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PMID:Effect of microbial phytase on energy availability, and lipid and protein deposition in growing swine. 1292 87


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