3.1.3.8: 3-phytase
This is an abbreviated version!
For detailed information about 3-phytase, go to the full flat file.
Word Map on EC 3.1.3.8
-
3.1.3.8
-
phosphorus
-
meal
-
broiler
-
ash
-
phytases
-
corn-soybean
-
agriculture
-
synthesis
-
phytic
-
barrows
-
tibia
-
allotted
-
housed
-
meal-based
-
digesta
-
quadratic
-
nonphytate
-
phytase-supplemented
-
equivalency
-
growing-finishing
-
nutrition
-
monogastric
-
excreta
-
indigestible
-
ficuum
-
dicalcium
-
chromic
-
manure
-
p-deficient
-
corn-based
-
gain:feed
-
phytate-p
-
grower
-
crates
-
maize-soybean
-
low-phosphorus
-
t-cannulas
-
6-phytase
-
phosphorus-deficient
-
monocalcium
-
phytate-degrading
-
food industry
-
as-fed
-
biotechnology
-
feedstuffs
-
cornstarch
-
wheat-based
-
analysis
-
metabolisable
- 3.1.3.8
- phosphorus
- meal
-
broiler
- ash
- phytases
-
corn-soybean
- agriculture
- synthesis
-
phytic
-
barrows
- tibia
-
allotted
-
housed
-
meal-based
-
digesta
-
quadratic
-
nonphytate
-
phytase-supplemented
-
equivalency
-
growing-finishing
- nutrition
-
monogastric
-
excreta
-
indigestible
- ficuum
-
dicalcium
-
chromic
-
manure
-
p-deficient
-
corn-based
-
gain:feed
-
phytate-p
-
grower
-
crates
-
maize-soybean
-
low-phosphorus
-
t-cannulas
- 6-phytase
-
phosphorus-deficient
-
monocalcium
-
phytate-degrading
- food industry
-
as-fed
- biotechnology
-
feedstuffs
-
cornstarch
-
wheat-based
- analysis
-
metabolisable
Reaction
Synonyms
1-phytase, 168phyA, 3'-phytase, 3-phytase, 3-phytase A, 3-phytase B, acid phytase, acidic histidine acid phosphatase, Afp, agpP, AgpP phytase, alkaline beta-propeller phytase, alkaline phytase, Allzyme, Allzyme phytase, AppA, appA phytase, AppA2, AppA2 phytase, AppAS, appA_Gw, Aspergillus niger N25 phytase, ASR1, AtPAP15, beta-propeller phytase, BIFPSEUDO_03792, Blon_0263, BPP, cell-bound phytase, cysteine phytase, dual-domain BPP, experimental phytase SP 1002, HAP, HAP phytase, HAP-phytase, histidine acid phosphatase, histidine acid phosphatase phytase, histidine acid phytase, HvPAPhy_a, LlALP1, LlALP2, microbial phytase, MiPhyA, MOK1 phytase, More, MYCTH_2306203, myo-inositol 1,2,3,4,5,6-hexakisphosphate phosphohydrolase, myo-inositol hexakiphosphate phosphohydrolase, myo-inositol hexakis phosphohydrolase, myo-inositol hexakisphosphate 3-phosphohydrolase, myo-inositol hexakisphosphate hydrolase, myo-inositol hexakisphosphate phosphohydrolase, myo-inositol hexaphosphate phosphohydrolase, myo-inositol-hexakisphosphate phosphohydrolase, MYO-inositol-hexaphosphate 3-phosphohydrolase, myo-inositol-hexaphosphate phosphohydrolase, myo-inositolhexakisphosphate phosphohydrolase, Natuphos, neutral phytase, NLP_0515, PAP, PAP type I, PAPhy, PAPhys, PAPhy_a1.1, pGF11 phytase, pGP209 phytase, pH 2.5 optimum acid phosphatase, Phy, PHY US42, PHY US573, phy168, PhyA, PhyA phytase, PhyA115, PhyA2, PhyB, PhyB49, PhyC, PhyCm, PhyH, PhyH49, PhyK, phyL, PhyP, phyS, phytase, phytase A, phytase C, phytate 1-phosphatase, Phytate 3-phosphatase, phytate 6-phosphatase, PhyTX52, PJ3 phytase, PPHY, protease-resistant phytase, PSphy, purple acid phosphatase, RMPhy1, RO1, RO2, Ronozyme P, RPHY1, ruminant microbial phytase, St-Phy, StPhy, tfphyA, YeAPPA, YkAPPA, YmPh
ECTree
3.1.3.8 3-phytaseAdvanced search results
results (
results (Source Tissue
Source Tissue on EC 3.1.3.8 - 3-phytase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
-
thermotolerant phytase is produced by Rhizopus microsporus var. microsporus biofilm on an inert support using sugarcane bagasse as carbon source. The enzyme production is strictly regulated by the phosphorus content with optimal production at 0.5 mM of sodium phytate and KH2PO4
recombinant enzyme in culture medium of Bacillus subtilis
barley plants constitutively express HvPAPhy_a, high preformed phytase levels in the mature dry vegetative material of the 35S:PAPhy_a-plant. Expression analysis in different plant tissues, overview. Positive correlation between phytase activity and plants being heterozygous or homozygous for the HvPAPhy_a cisgene (the genomic clone of HvPAPhy_a including the native promoter and terminator of the gene)
additional information
-
phytase increases markedly at the late stationary phase
-
fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml
Rhodotorula mucilaginosa JMUY14
-
fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml
-
-
phytase synthesized early in germination persists for several days in the cotyledon
solid-state fermentation, optimization of enzyme phytase production by Sporotrichum thermophile, method, detailed overview. Maximum phytase production (1881.26 U/g dry mouldy residue) in 2.5% Tween 80, 1.0% yeast extract, and 48 h of incubation period. Phytase production in the mixed substrate (sugarcane bagasse and wheat bran) fermentation enhances 11.6fold over the initial production as a consequence of optimization. Phytase titres are sustainable in flasks, trays and column bioreactor (1796 to 2095 U/g dry mouldy residue), thus validating the model and the process for large-scale phytase production. When the yeast extract is replaced with corn steep liquor (2% w/v), a sustained enzyme titre (1890 U/g dry mouldy residue) is attained, making the process cost-effective. Among all the detergents, Tween 80 supports a higher phytase production than others. The enzyme efficiently liberates nutritional components from poultry feed (inorganic phosphate, soluble protein and reducing sugars) in a time-dependent manner
Thermothelomyces thermophilus BJTLR50
-
solid-state fermentation, optimization of enzyme phytase production by Sporotrichum thermophile, method, detailed overview. Maximum phytase production (1881.26 U/g dry mouldy residue) in 2.5% Tween 80, 1.0% yeast extract, and 48 h of incubation period. Phytase production in the mixed substrate (sugarcane bagasse and wheat bran) fermentation enhances 11.6fold over the initial production as a consequence of optimization. Phytase titres are sustainable in flasks, trays and column bioreactor (1796 to 2095 U/g dry mouldy residue), thus validating the model and the process for large-scale phytase production. When the yeast extract is replaced with corn steep liquor (2% w/v), a sustained enzyme titre (1890 U/g dry mouldy residue) is attained, making the process cost-effective. Among all the detergents, Tween 80 supports a higher phytase production than others. The enzyme efficiently liberates nutritional components from poultry feed (inorganic phosphate, soluble protein and reducing sugars) in a time-dependent manner
-
-
strong expression in the early stages of seedling growth and pollen germination
-
both phytase and acid phosphatase enzyme activities in the root increase substantially in response to phosphorus-sufficient condition. The lowest enzyme activity is observed in the absence of any phosphorus source in the media. The level of acid phosphatase and phytase activities is more or less the same under various growth conditions
quantitative reverse transcription PCR enzyme expression analysis in developing grains
quantitative reverse transcription PCR enzyme expression analysis in developing grains
-
quantitative reverse transcription PCR enzyme expression analysis in developing grains
-
-
strong expression in the early stages of seedling growth and pollen germination
additional information
enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus source. Phytase production by strain a13 is induced by the presence of phytic acid and repressed by the addition of glucose
additional information
Burkholderia sp. a13(2014) JCM 30421
-
enrichment cultivation using minimum medium containing phytic acid as the sole phosphorus source. Phytase production by strain a13 is induced by the presence of phytic acid and repressed by the addition of glucose
-
additional information
-
optimization of process parameters for phytase production by Enterobacter sp. ACSS leads to a 4.6fold improvement in submerged fermentation, which is enhanced further in fed-batch fermentation
additional information
ability of the Pantoea sp. 3.5.1 isolate to grow with insoluble Ca-phytate as the sole source of phosphorus, not due to the secretion of an extracellular phytase. Growth dynamics and extracellular and intracellular phytate-hydrolyzing activities of Pantoea sp. 3.5.1 culture, overview
additional information
-
growth on rice flour suspension or on potato dextrose agar
additional information
the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations
additional information
identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
additional information
identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
additional information
-
identification of wheat phytase in mature and germinating grains by tandem mass spectrometry analysis
-
additional information
-
among 10 yeast strains analyzed, Arxula adeninivorans and Pichia anomala display highest volumetric phytase activities
additional information
optimization of fermentation for production of cell-bound phytase, overview
additional information
-
optimization of fermentation for production of cell-bound phytase, overview
