Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.8 (phytase)
 1,997 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The effects of phosphorus deprivation on phytate digestibility, phosphorus utilization and intestinal phytase (EC 3.1.3.8) and alkaline phosphatase (EC 3.1.3.1) in rats were investigated. 2. P deprivation was achieved by giving rats a diet containing 3 g P/kg and resulted in hypophosphataemia, hypercalcaemia, hypercalciuria, and lower levels of P absorbed and retained, and calcium retained. 3. Rats adapted to P deprivation by increasing the digestion of total dietary-P and phytate-P. 4. Levels of intestinal alkaline phosphatase and alkaline phytase were not different between the two treatment groups. 5. P deprivation in the rats given the marginal-P diet may be a result of a lower absorption of total dietary-P or increased absorption of inositol phosphates formed during the enzymatic hydrolysis of phytate which are not readily utilized by the rat. 6. These results suggest that intestinal phytase and alkaline phosphatase do not play a role in the adaptive increase in phytate digestibility by rats given marginal-P diets. The adaptation may result from enhanced phytase or alkaline phosphatase synthesis by the gastrointestinal microflora stimulated by a lower level of P in the digesta.
 ...
PMID:Adaptive increase in phytate digestibility by phosphorus-deprived rats and the relationship of intestinal phytase (EC 3.1.3.8) and alkaline phosphatase (EC 3.1.3.1) to phytate utilization. 629 37

The effects of vitamin D-deficiency and repletion on the distribution and activities of Ca2+-ATPase, phytase, and alkaline phosphatase in intact epithelial cells isolated from different regions of the villi and the crypts of the rat jejunum were studied. Similar distribution patterns of activities were found for the three enzymes. In all cases, the enzyme levels were the highest at the villus tip and gradually declined to low activities in the crypt. The Kms were very different between cells in the crypt base and those at the villus tip, the highest Kms being found in the crypt. The activities of these enzymes were reduced in the entire length of the villus in vitamin D-deficient rats. Recovery of the enzymatic levels was observed on vitamin D repletion, but at different rates. Total recovery of activity of Ca2+-ATPase, phytase, and alkaline phosphatase was observed after 18, 24, and 36 hours, respectively, after a single dose of 6.5 nmol (2.5 micrograms) vitamin D3. Enzymatic activities in the crypt cells were not affected by vitamin D3 treatment. These data suggest that Ca2+-ATPase, phytase, and alkaline phosphatase may be distinct entities, and that their activities in the crypt cells may not be vitamin D-dependent.
 ...
PMID:Distribution and properties of Ca2+-ATPase, phytase, and alkaline phosphatase in isolated enterocytes from normal and vitamin D-deficient rats. 631 91

Phytase (EC 3.1.3.8) concentration has been measured in the small intestine of rat, rabbit, guinea-pig and hamster. Levels varied from 0.12 units (microgram phosphorus released/min)/mg protein in the rat to 0.03 units/mg protein in the rabbit. The enzyme is localized in the brush border of the small intestine of the rat. It is suggested that the levels and location of phytase are an important factor in the uptake of metals from metal-phytate complexes. Metal ions released in the immediate vicinity of the absorptive surface of the intestine could be absorbed before being rendered insoluble by competing reactions such as hydrolysis.
 ...
PMID:Mammalian small intestinal phytase (EC 3.1.3.8). 631 52

The effects of dietary phosphorus and sulphaguanidine levels, and sex differences on: (a) phytate digestibility, (b) calcium and P utilization, (c) the activities of alkaline phosphatase (EC 3.1.3.1), alkaline phytase (EC 3.1.3.8) and acid phosphatase (EC 3.1.3.2) in the intestinal mucosa of male and female rats were investigated. There was a linear increase in femur ash, Ca and P contents and the maximum force withstood by the fresh femurs as dietary P level was increased from 1.5 to 3.0 to 4.5 g/kg diet. The apparent digestibilities of Ca, P and phytate-P decreased as the level of P in the diet increased. Rats given the diets with 1.5 or 3.0 g P/kg were hypercalciuric and hypophosphaturic compared with rats receiving 4.5 g P/kg diet. The level of Ca retained was similar for all treatments. The level of P retained increased as the dietary P level increased. This suggests that P deprivation was a result of inadequate amounts of P retained and not due to the absorption of inositol phosphates formed during the enzymic hydrolysis of phytate. The addition of sulphaguanidine increased phytate digestibility without changing the activities of acid and alkaline phosphatase or alkaline phytase of the intestinal mucosa. This suggests that these enzymes did not play a role in the increase in phytate digestibility. However, dietary sulphaguanidine enhanced phytate digestibility, suggesting that alterations in the diet which modify either the composition or metabolism of the gastrointestinal microflora may be beneficial in enhancing the in vivo hydrolysis of phytate. Differences between males and females are reported and discussed.
 ...
PMID:Influence of dietary phosphorus and sulphaguanidine levels on P utilization in rats. 632 99

Phytic acid is present in many plant systems, constituting about 1 to 5% by weight of many cereals and legumes. Concern about its presence in food arises from evidence that it decreases the bioavailability of many essential minerals by interacting with multivalent cations and/or proteins to form complexes that may be insoluble or otherwise unavailable under physiologic conditions. The precise structure of phytic acid and its salts is still a matter of controversy and lack of a good method of analysis is also a problem. It forms fairly stable chelates with almost all multivalent cations which are insoluble about pH 6 to 7, although pH, type, and concentration of cation have a tremendous influence on their solubility characteristics. In addition, at low pH and low cation concentration, phytate-protein complexes are formed due to direct electrostatic interaction, while at pH > 6 to 7, a ternary phytic acid-mineral-protein complex is formed which dissociates at high Na+ concentrations. These complexes appear to be responsible for the decreased bioavailability of the complexed minerals and are also more resistant to proteolytic digestion at low pH. Development of methods for producing low-phytate food products must take into account the nature and extent of the interactions between phytic acid and other food components. Simple mechanical treatment, such as milling, is useful for those seeds in which phytic acid tends to be localized in specific regions. Enzyme treatment, either directly with phytase or indirectly through the action of microorganisms, such as yeast during breadmaking, is quite effective, provided pH and other environmental conditions are favorable. It is also possible to produce low-phytate products by taking advantage of some specific interactions. For example, adjustment of pH and/or ionic strength so as to dissociate phytate-protein complexes and then using centrifugation or ultrafiltration (UF) has been shown to be useful. Phytic acid can also influence certain functional properties such as pH-solubility profiles of the proteins and the cookability of the seeds.
 ...
PMID:Phytic acid interactions in food systems. 700 70

Soaking of a rat diet, high in both plant phytate and phytase, progressively degraded the phytate content with time of soaking. This dephytinization in turn enhanced the digestion of feed organic matter in the animals, and it significantly improved the absorption and retention of minerals and trace elements as observed in balance studies. Incorporation of elements into specific tissues was evaluated as a reflection of bioavailability. Some tissues did reflect the preceding absorption of certain elements; other tissues seemed less suitable as indicators of trace element absorption. Dietary calcium addition in many ways contrasted the soaking procedure: inorganic calcium addition to the feed reduced phosphorus, magnesium, and trace element bioavailability, and interfered with the internal deposition of the elements. The external dephytinization of the feed did not affect the phosphohydrolase activity of the intestinal mucosa as manifested by alkaline phosphatase activity or phytase activity. The mucosal phytase and alkaline phosphatase activities were, however, mutually correlated, supporting the view that "phytase" activity is a less substrate-specific action of alkaline phosphatase activity or a fraction of this activity.
 ...
PMID:Dephytinization of a rat diet. Consequences for mineral and trace element absorption. 750

An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4) on phytate dephosphorylation. Pepsin (EC 3.4.23.1) and pancreatin digestion periods were preceded by a 30 min pre-incubation at pH 5.25 to simulate digestion in the crop of poultry. Pancreatin digestion was carried out in dialysis tubing, with a ratio of about 1:25 (v/v) between the digesta and dialysing medium, to simulate gradient absorption from the duodenum. The feed:water ratio was kept within physiological limits and a constant proportion of feed weight to digestive enzymes was maintained. There was a linear response to increasing dosages of phytase up to 1000 phytase units (FTU)/kg feed, and to increasing phosphate concentration in feeds. In vivo validation was performed with growing turkeys (1-3 weeks) fed on diets containing 12 g Ca/kg and 0, 500 or 1000 FTU phytase/kg in a factorial arrangement with 0, 1, 2 or 3 g supplemental phosphate/kg (from KH2PO4). After a simple transformation (variable/in vitro P = f (in vitro P)), amounts of P hydrolysed from feed samples by in vitro digestions correlated with 3-week body-weight gain (R 0.986, P < 0.0001), toe ash (R 0.952, P < 0.0001), feed intake (R 0.994, P < 0.0001) and feed efficiency (R 0.992, P < 0.0001). The dephosphorylating ability of phytase in vitro was significantly enhanced (P < 0.05) by the addition of acid phosphatase. Fungal acid protease and Aspergillus niger cellulase also enhanced the dephosphorylation process in vitro.
 ...
PMID:An in vitro procedure for studying enzymic dephosphorylation of phytate in maize-soyabean feeds for turkey poults. 754 27

Three experiments involving 162 pigs were conducted to assess the efficacy of phytase (Natuphos; BASF, Mount Olive, NJ) in low-P, corn-soybean meal-based diets. The phytase was produced by a recombinant Aspergillus niger. The phytase supplement contained 5,000 phytase units (PTU)/g. In Exp. 1 (66 pigs) and 2 (60 pigs), growing-finishing pigs were fed fortified corn-soybean meal diets formulated to be adequate (.50%), marginal (.425%), or inadequate (.35%) in P during the growing phase (23 to 60 kg BW) followed by adequate (.40%), marginal (.35%), or inadequate (.30%) P, respectively, during the finishing phase (to 104 kg BW). Dicalcium phosphate was the source of supplemental P. In addition, the low-P sequence (.35/.30% P) was supplemented with phytase at 250, 500, or 1,000 PTU/kg. Rate and efficiency of gain decreased linearly (P < .01) and bone breaking strength decreased quadratically (P < .01) as the concentration of P was decreased in the diets. Responses in growth and bone traits to increasing levels of phytase activity in the low-P diet were linear (P < .01). The highest level of phytase in the low-P diet restored growth rate and bone breaking strength to levels that approached or met those of pigs fed the adequate P diet.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Efficacy of a recombinant-derived phytase in improving the bioavailability of phosphorus in corn-soybean meal diets for pigs. 759 84

Two experiments involving 115 pigs were conducted to assess the efficacy of a microbial phytase (Allzyme Phytase; Alltech, Nicholasville, KY) produced by Aspergillus niger in low-P, corn-soybean meal-based diets. The phytase supplement contained 50 phytase units/g and 1.43% P. In Exp. 1, growing-finishing pigs were fed fortified corn-soybean meal diets formulated to be adequate (.50%) or inadequate (.30%) in P during the growing phase (38 to 57 kg BW) followed by adequate (.40%) or inadequate (.30%) P, respectively, during the finishing phase (to 101 kg BW). Dicalcium phosphate was the source of supplemental P. Half the diets were supplemented with phytase at 500 phytase units/kg. Rate and efficiency of gain and bone breaking strength were decreased (P < .01) when the low-P diet was fed. Adding phytase to the low-P diet restored performance and bone breaking strength (P < .01) to levels that approached those of pigs fed the adequate-P diet. In Exp. 2, growing pigs (13 kg BW), were fed a low-P (.32% total P; .048% available P) based diet supplemented with graded levels of monosodium phosphate to provide 0, .075, and .15% added P or with phytase to supply 250, 500, 1,000, or 2,000 phytase units/kg. Chromic oxide was included as an indigestible marker for determining apparent absorption and fecal excretion of P. Performance and bone strength increased linearly with added monosodium phosphate (P < .01) and with increasing levels of supplemental phytase (P < .05). A portion of these increases from phytase was attributed to the P supplied by the phytase mix (.007, .014, .028, .057%, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Efficacy of low-activity, microbial phytase in improving the bioavailability of phosphorus in corn-soybean meal diets for pigs. 760 78

Four acid phosphatase (phosphomonoesterase E.C.3.1.3.2) genes were cloned by polymerase chain reaction (PCR). These were pho3, pho5 and pho11 from Saccharomyces cerevisiae and the gene for a phosphate-respressible acid phosphatase from Aspergillus niger. The individual genes were subcloned into an A. oryzae expression vector downstream from a starch-inducible alpha-amylase promoter and the resulting expression constructs were transformed into a mutant strain of A. oryzae, AO7. Southern hybridization analysis confirmed that the acid phosphatase genes had been integrated into the host genome with estimates of integrated copy numbers ranging from 2 to 20 for individual transformants. Northern hybridization analysis of total RNA from individual transformants revealed the presence of a single transcript of the expected size of 1.8 kb. Production of recombinant protein was induced by the addition of 30 g L-1 of soluble starch in the fermentation media. Active acid phosphatases, not present in control cultures, were detected in the supernatant fractions of transformant cultures by acid phosphatase activity staining of non-denaturing polyacrylamide gels. The ability of the recombinant acid phosphatases to hydrolyze phytate was assessed by referenced phytase (myoinositol hexakisphosphate phosphohydrolase E.C. 3.1.3.8) activity assay procedures. A two- to six-fold increase in phytase activity was measured in transformants compared to control, untransformed A. oryzae. Sufficient quantities of A. niger and pho5 recombinant acid phosphatases were generated from large-scale fermentations to assess the efficacy of these enzymes as phytate-degrading enzymes when included in poultry diets.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Molecular cloning, expression and evaluation of phosphohydrolases for phytate-degrading activity. 761 16


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>