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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)

The changes promoted by germination on phytates, oligosaccharides, crude protein, amino acids and riboflavin contents of black and white cultivars of beans, lentils, chicken-pea and peas, were studied. Seeds germination was carried out in darkness at 25 degrees C and 85% RH during 72 hours, previously soaked overnight in a solution of sodium hypochlorite at a concentration of 50 ppm. Germination capacity was assessed by determining hypocotyl and epicotyl lengths and percent of sprouted seed. The seeds were milled and freeze-dried for the chemical analysis. Germination promoted a significant increase in crude protein content and reduction also significant in phytates levels. These changes were attributed to an increase of proteases and phytase activities. In fact, this enzyme would make a solubilization of phytates and would release soluble protein and minerals. A significant reduction of flatulence oligosaccharides took place, which was also explained by an increase of alpha-galactosidase concentration. Sprouted seeds showed a higher content of almost all amino acid than crude legumes, although this change was variable. Significant increase of riboflavin was also found. Finally, germination decreased ashes and fat contents. These findings were determined in all legumes, although both cultivars of beans showed a higher response to the biochemical changes.
Arch Latinoam Nutr 1992 Sep
PMID:[Nutritional changes caused by the germination of legumes commonly eaten in Chile]. 134 62

Phytase (myo-inositol hexakisphosphate phosphohydrolase; EC 3.1.3.8 or 3.1.3.26) was purified from rat intestinal mucosa. The purified enzyme preparation exhibited two protein bands on SDS-polyacrylamide gel electrophoresis with estimated molecular masses of 70 kDa and 90 kDa. Rabbit antisera prepared against the 90K subunit cross-reacted with the 70K subunit on immunoblotting. The peptide maps of the 70K and 90K subunits were similar, and the N-terminal amino acid sequences of the two subunit proteins were almost identical. Treatments to remove sugar moieties from the proteins showed that the two subunit proteins had different oligosaccharide chains, although the difference in their molecular masses was not due to the difference in their oligosaccharide compositions. The purified enzyme also showed activity of alkaline phosphatase (orthophosphoric monoester phosphohydrolase; EC 3.1.3.1), but the properties of the two enzyme activities were different; the optimum pH for phytase activity was 7.5, while that for alkaline phosphatase was 10.4. Phytase activity did not necessarily require divalent cations, while Mg2+ was essential for alkaline phosphatase activity. Phenylalanine, a specific inhibitor of intestine-type alkaline phosphatase had no effect on the phytase activity.
Biochim Biophys Acta 1991 Sep 02
PMID:Purification and characterization of phytase from rat intestinal mucosa. 165 10

The activities of phytase and alkaline phosphatase in the intestine gradually increased in parallel during development of rats, but the 70K and 90K subunits were expressed differentially; only the 70K subunit was detected at birth, whereas the 90K subunit appeared at the weaning period (3 weeks after birth). When rats were forced to wean at 18 days old and fed laboratory chow, the enzyme activity increased markedly and the 90K subunit appeared within 1 day. These findings suggest that weaning is involved in the change in the subunit composition. Increases in the enzyme activity and amount of the 90K subunit were significantly delayed by feeding weanling animals on casein diet, but induced significantly by feeding them on casein diet supplemented with phytate. Thus induction of the 90K subunit seems to be accelerated by intake of phytic acid in the diet. The Km value of the enzyme from suckling rats for phytate was 5.25 mM, while that of adult rats was 0.213 mM. In contrast, the Km value for p-nitrophenyl phosphate (PNPP) was constant during development. The phytase activity of suckling rats did not show a distinct pH-dependence. These findings suggest that the 90K subunit may play some important roles in expressing an efficient phytase activity.
Biochim Biophys Acta 1991 Sep 02
PMID:Developmental and dietary induction of the 90K subunit of rat intestinal phytase. 165 11

Techniques have been developed to produce microbial phytase for addition to diets for simple-stomached animals, with the aim to improve phosphorus availability from phytate-P in plant sources. The activity of the crude microbial phytase showed pH optima at pH 5.5 and 2.5. The enzyme was able to degrade phytate in vitro in soya-bean meal, maize and a liquid compound feed for pigs. When microbial phytase was added to low-P diets for broilers the availability of P increased to over 60% and the amount of P in the droppings decreased by 50%. The growth rate and feed conversion ratio on the low-P diets containing microbial phytase were comparable to or even better than those obtained on control diets. Addition of microbial phytase to diets for growing pigs increased the apparent absorbability of P by 24%. The amount of P in the faeces was 35% lower.
Br J Nutr 1990 Sep
PMID:Improvement of phosphorus availability by microbial phytase in broilers and pigs. 1570 36

The role of bacterial, dietary and intestinal phytases (EC 3.1.3.8) in the hydrolysis of phytate was investigated in the golden hamster and rat by assaying phytase in the small intestine and by measuring the disappearance of phytate from the stomach and large intestine, using chromium oxide as an insoluble solid-phase marker. It was confirmed that an active phytase was present in the proximal third of the small intestine of the rat but the enzyme was undetectable in the hamster. Extensive bacterial breakdown of phytate occurred in the pregastric pouch and true stomach of the hamster with both phytase-containing and phytase-free diets, with phytate digestibilities in the true stomach ranging from 0.69-0.90, confirming that the hamster can be regarded as a pseudo-ruminant. With a phytase-free diet, the digestibility of phytate in the stomach of the rat was very low (0.05) but with a wheat-based diet substantial breakdown of phytate occurred (digestibility up to 0.49), presumably under the influence of the cereal phytase. Intestinal phytase did not appear to be of great significance in the rat but some further hydrolysis of the residual phytate probably occurred in the large intestine of both species by bacterial phytase.
Br J Nutr 1985 Sep
PMID:A comparative study of phytate hydrolysis in the gastrointestinal tract of the golden hamster (Mesocricetus auratus) and the laboratory rat. 406 29

A culture enrichment technique was used to isolate phytase-producing microorganisms. Also, microorganisms from various culture collections were tested for their phytase-producing ability. A number of the Aspergillus niger group produced extracellular phytase which dephosphorylated calcium phytate in acidic solution. A soil isolate, A. ficuum NRRL 3135, produced the most active phytase in a cornstarch-based medium. Production of phytase was strongly repressed by inorganic phosphates and required a high carbon to phosphorus ratio in the medium.
Appl Microbiol 1968 Sep
PMID:Survey of microorganism for the production of extracellular phytase. 430 Jan 71

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.
J Bacteriol 1982 Sep
PMID:Purification and properties of phytate-specific phosphatase from Bacillus subtilis. 628 90

Seven experiments were conducted to determine the efficacy of 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] and microbial phytase in improving P, Zn and Mn utilization of chicks fed P, Zn- and Mn-deficient soy protein diets containing surfeit levels of cholecalciferol. Efficacy of 1 alpha-hydroxycholecalciferol (1 alpha-OH D3) was also studied. A dose titration study indicated that supplemental phytase at 1200 units/kg diet would increase bone ash by at least 65% when added to a corn-soybean meal diet containing 0.43 g P/100 g (0.1 g nonphytate P/100 g). These responses were similar to those obtained from supplemental P (0.1 g/100 g) as KH2PO4 or from added 1,25-(OH)2D3 (10 micrograms/kg). Dietary addition of both 1200 units phytase and 10 micrograms/kg 1,25-(OH)2D3 elicited bone ash responses that were near 100%. When chicks were fed a Zn-deficient soy-concentrate diet (13 mg Zn/kg), diet supplementation with 1,25-(OH)2D3 or phytase increased growth rate by 40% and tibia Zn content by > 100%; adding 1,25-(OH)2D3 together with phytase increased tibia Zn content by 160%. Utilization of both Zn and Mn contained in the corn-soybean meal diet also was markedly enhanced by supplemental phytase, 1,25-(OH)2D3, or the combination. The cholecalciferol analog 1 alpha-OH D3 was found to improve dietary P utilization maximally (70% bone ash response) at a dose of 20 micrograms/kg diet, and effects were additive when 1 alpha-OH D3 was fed in the presence of phytase.(ABSTRACT TRUNCATED AT 250 WORDS)
J Nutr 1995 Sep
PMID:1 alpha-Hydroxylated cholecalciferol compounds act additively with microbial phytase to improve phosphorus, zinc and manganese utilization in chicks fed soy-based diets. 766 60

Capillary isotachophoresis with conductivity detection was applied to the investigation of the hydrolytic decomposition of phytic acid (myo-inositol hexaphosphoric acid) by phytase, and for the formation of the reaction products as a function of time. The quantitation of all analytes (besides phytic acid the mono- to penta-phosphorylated inositols and orthophosphate) can be carried out using two different buffer systems.
J Chromatogr A 1994 Sep 23
PMID:Time course of formation of inositol phosphates during enzymatic hydrolysis of phytic acid (myo-inositol hexaphosphoric acid) by phytase determined by capillary isotachophoresis. 795 96

Phytate is the major storage form of phosphorus in seeds and so is a common dietary constituent. Excessive ingestion of undegraded phytates can cause mineral deficiencies in humans. In addition, phytic acid is antineoplastic in animal models of both colon and breast carcinoma. There have been no previous studies quantifying phytase activity in the human small intestine although it is present in animals. Small intestinal phytase and alkaline phosphatase activity and distribution was measured in vitro in mucosal homogenates from two human small intestinal specimens obtained from transplant donors. Rat intestine was also studied for comparison. Phytase activity was found in human small intestine at low values (30 times less than that in rat tissue and 1000-fold lower than alkaline phosphatase in the same tissue). The activity was greatest in the duodenum and lowest in the ileum. In conclusion, the normal human small intestine has very limited ability to digest undegraded phytates. Although this may have adverse nutritional consequences with respect to metabolic cation imbalances, the presence of undigested phytate in the colon may protect against the development of colonic carcinoma.
Gut 1994 Sep
PMID:Phytase activity in the human and rat small intestine. 795 29


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