Application | Comment | Organism |
---|---|---|
biotechnology | phytase from Bacillus subtilis (168phyA) is constitutively expressed in tobacco and Arabidopsis to generate transgenic plants capable of utilizing exogenous phytate. In tobacco, phytase activities in transgenic leaf and root extracts are seven to eight times higher than those in wild-type extracts; whereas, the extracellular phytase activities of transgenic plants are enhanced by four to six times. Similar results are observed from the transgenic Arabidopsis. These results may offer a new perspective on mobilizing soil phytate into inorganic phosphate for plant uptake | Bacillus subtilis |
biotechnology | phytase from Bacillus subtilis is introduced into the cytoplasm of tobacco cells that results in equilibrium shift of inositol biosynthesis pathway, thereby making more phosphate available for primary metabolism. The transgenic line exhibit phenotypic changes like increased flowering, lower seed IP6/IP5 ratio, and enhanced growth under phosphate starvation conditions compared to wild type | Bacillus subtilis |
biotechnology | phytase is very suitable to be used in animal feed particularly in common carp feed because of its optimum pH with excellent thermal stability. Bacillus phytase supplementation of 300 U/kg can gain the same result as that of 1000 U/kg supplementation of acidic phytase and neutral phytase supplementation of 1000 U/kg can replace the inorganic phosphorus supplement. A combination of Bacillus phytases and other acidic phytases might induce a more effective hydrolysis of phytate in both the stomach and small intestine of animals in terms of the pH of the animal gastrointestinal tract | Bacillus sp. (in: Bacteria) |
Cloned (Comment) | Organism |
---|---|
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability | Bacillus subtilis |
overexpressed the phytase gene phyL from Bacillus licheniformis and phytase gene (168phyA) identified from Bacillus subtilis strain 168 in Bacillus subtilis using a omega105MU331 prophage vector system. Up to 35 U/ml are secreted into the culture media. Both phytases exhibit broad temperature and pH optima and show high thermal stability | Bacillus licheniformis |
Crystallization (Comment) | Organism |
---|---|
crystal structure of the phytase from Bacillus amyloliquefaciens DS11 demonstrate that a negatively charged active site provides a favorable electrostatic environment for the positively charged calcium-phytate complex | Bacillus amyloliquefaciens |
determined at 2.1 A resolution in partially and fully Ca2+-loaded states. Two calcium ions form a biocalcium center where the Asp308 carboxylate serves as a bridging arm, stabilizing the circular arrangement of the propeller structure. Three calcium ions at the active site form a triadic calcium center and neutralize an otherwise negatively charged calcium cage surrounded by a total of six aspartate and glutamate residues. The top of the molecular structure forms a shallow cleft that is lined predominantly with negatively charged side chains. The calcium-occupied cleft turns into a favorable electrostatic environment for the binding of phytate together with nearby Lys76, Lys77, Arg122, and Lys179. In addition, Ca2+ participates in catalysis directly by binding the phosphate group(s) of the substrate. Ca2+ reduces the negative charge around the active site cleft such that phytate neutralized by Ca2+ can easily fit to the active site | Bacillus amyloliquefaciens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Bacillus sp. (in: Bacteria) | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | enhances thermal stablity and shows an impact on pH-optimum and temperature optimum | Bacillus sp. (in: Bacteria) |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36000 | - |
molecular weight: 36 - 38 kDa | Bacillus subtilis |
36500 | - |
- |
Bacillus subtilis |
44000 | - |
- |
Bacillus sp. (in: Bacteria) |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus amyloliquefaciens | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Bacillus licheniformis | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Bacillus sp. (in: Bacteria) | - |
- |
- |
Bacillus sp. (in: Bacteria) | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Bacillus sp. (in: Bacteria) KHU-10 | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Bacillus subtilis | - |
- |
- |
Bacillus subtilis | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Sporolactobacillus laevolacticus | - |
the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
specific activity of the purified protein: 8.5-9 U/mg | Bacillus subtilis |
additional information | - |
specific activity of the purified protein: 8.7 U/mg | Bacillus subtilis |
additional information | - |
specific activity of the purified protein: 8.7 U/mg | Bacillus sp. (in: Bacteria) |
additional information | - |
specific activity of the purified protein: 8.7 U/mg | Sporolactobacillus laevolacticus |
Synonyms | Comment | Organism |
---|---|---|
(natto) phytase | - |
Bacillus subtilis |
(natto) phytase | - |
Bacillus sp. (in: Bacteria) |
168phyA | - |
Bacillus subtilis |
phyL | - |
Bacillus licheniformis |
phytase | - |
Bacillus subtilis |
phytase | - |
Bacillus sp. (in: Bacteria) |
phytase | - |
Bacillus amyloliquefaciens |
phytase | - |
Sporolactobacillus laevolacticus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
without 10 mM CaCl2 | Bacillus sp. (in: Bacteria) |
60 | - |
- |
Bacillus subtilis |
60 | - |
with 10 mM CaCl2 | Bacillus sp. (in: Bacteria) |
70 | - |
- |
Sporolactobacillus laevolacticus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
phyL exhibits high thermal stability, even at a lower calcium concentration, as it is able to recover 80% of its original activity after denaturation at 95 °C for 10 min | Bacillus licheniformis |
70 | - |
80% activity at 70°C and pH 8.0 for up to 3 h | Sporolactobacillus laevolacticus |
70 | - |
enzyme is stable up to 70°C | Bacillus subtilis |
80 | - |
about 50% of its original activity remains after incubation at 80°C for 10 min in the presence of 10 mM CaCl2 | Bacillus sp. (in: Bacteria) |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 6.5 | - |
Bacillus subtilis |
6.5 | 8.5 | without 10 mM CaCl2 | Bacillus sp. (in: Bacteria) |
6.5 | 9.5 | with 10 mM CaCl2 | Bacillus sp. (in: Bacteria) |
7 | 8 | - |
Sporolactobacillus laevolacticus |
7 | 7.5 | - |
Bacillus subtilis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6.5 | 10 | - |
Bacillus sp. (in: Bacteria) |