Any feedback?
Literature summary extracted from
- Expression of bifidobacterial phytases in Lactobacillus casei and their application in a food model of whole-grain sourdough bread (2016), Int. J. Food Microbiol., 216, 18-24 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | food industry | the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes | Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | food industry | the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes | Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | food industry | the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | food industry | the constructed engineered Lactobacillus casei strain is applied as starter in a bread making process using whole-grain flour. Lactobacillus casei develops in sourdoughs by fermenting the existing carbohydrates giving place to an acidification. In this food model system the contribution of Lactobacillus casei strains expressing phytases to phytate hydrolysis is low, and the phytate degradation is mainly produced by activation of the cereal endogenous phytase as a consequence of the drop in pH. Capacity of lactobacilli to be modified in order to produce enzymes with relevance in food technology processes | Bifidobacterium longum subsp. infantis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | gene Blon_0263, recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, but the Bifidobacterium longum enzyme is not expressed or it is expressed at a low level | Bifidobacterium longum subsp. infantis |
| 3.1.3.8 | gene phy, functional recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, the Bifidobacterium pseudocatenulatum is efficiently expressed | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | gene Blon_0263, recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, but the Bifidobacterium longum enzyme is not expressed or it is expressed at a low level | Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | gene phy, functional recombinant expression in Lactobacillus casei strain BL23 under the control of a nisin-inducible promoter, subcloning in Lactobacillus lactis strain MG1363, the Bifidobacterium pseudocatenulatum is efficiently expressed | Bifidobacterium pseudocatenulatum |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.8 | membrane | integral membrane protein | Bifidobacterium pseudocatenulatum | 16020 | - |
| 3.1.3.8 | membrane | integral membrane protein | Bifidobacterium longum subsp. infantis | 16020 | - |
| 3.1.3.26 | membrane | integral membrane protein | Bifidobacterium pseudocatenulatum | 16020 | - |
| 3.1.3.26 | membrane | integral membrane protein | Bifidobacterium longum subsp. infantis | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | Bifidobacterium pseudocatenulatum | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? |  |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis S12 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis JCM 1222 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis NCTC 11817 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis DSM 20088 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium longum subsp. infantis ATCC 15697 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | additional information | Bifidobacterium pseudocatenulatum ATCC 27919 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Bifidobacterium pseudocatenulatum | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium pseudocatenulatum | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis S12 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis JCM 1222 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis NCTC 11817 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis DSM 20088 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium longum subsp. infantis ATCC 15697 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | additional information | Bifidobacterium pseudocatenulatum ATCC 27919 | effect of sourdough on the myo-inositol phosphates levels, overview | ? | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium pseudocatenulatum | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis S12 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis JCM 1222 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis NCTC 11817 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis DSM 20088 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium longum subsp. infantis ATCC 15697 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | Bifidobacterium pseudocatenulatum ATCC 27919 | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Bifidobacterium longum subsp. infantis | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium longum subsp. infantis ATCC 15697 | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium longum subsp. infantis DSM 20088 | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium longum subsp. infantis JCM 1222 | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium longum subsp. infantis NCTC 11817 | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium longum subsp. infantis S12 | B7GTV0 | - |
- |
| 3.1.3.8 | Bifidobacterium pseudocatenulatum | C0BTR1 | - |
- |
| 3.1.3.8 | Bifidobacterium pseudocatenulatum ATCC 27919 | C0BTR1 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis ATCC 15697 | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis DSM 20088 | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis JCM 1222 | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis NCTC 11817 | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium longum subsp. infantis S12 | B7GTV0 | - |
- |
| 3.1.3.26 | Bifidobacterium pseudocatenulatum | C0BTR1 | - |
- |
| 3.1.3.26 | Bifidobacterium pseudocatenulatum ATCC 27919 | C0BTR1 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium pseudocatenulatum | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium pseudocatenulatum | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis S12 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis S12 | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis JCM 1222 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis JCM 1222 | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis NCTC 11817 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis NCTC 11817 | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis DSM 20088 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis DSM 20088 | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis ATCC 15697 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis ATCC 15697 | ? | - |
? | |
| 3.1.3.8 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium pseudocatenulatum ATCC 27919 | ? | - |
? | |
| 3.1.3.8 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium pseudocatenulatum ATCC 27919 | ? | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium pseudocatenulatum | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium pseudocatenulatum | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium pseudocatenulatum | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis S12 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis S12 | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis JCM 1222 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis JCM 1222 | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis NCTC 11817 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis NCTC 11817 | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis DSM 20088 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis DSM 20088 | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium longum subsp. infantis ATCC 15697 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium longum subsp. infantis ATCC 15697 | ? | - |
? | |
| 3.1.3.26 | additional information | effect of sourdough on the myo-inositol phosphates levels, overview | Bifidobacterium pseudocatenulatum ATCC 27919 | ? | - |
? | |
| 3.1.3.26 | additional information | ammonium vanadate and ammonium molybdate staining method for activity determination. The recombinant enzyme produces myo-inositol pentakisphosphate, myo-inositol tetrakisphosphate, and myo-inositol triphosphate from myo-inositol hexakisphosphate, respectively | Bifidobacterium pseudocatenulatum ATCC 27919 | ? | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium pseudocatenulatum | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis S12 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis JCM 1222 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis NCTC 11817 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis DSM 20088 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium longum subsp. infantis ATCC 15697 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
| 3.1.3.26 | myo-inositol hexakisphosphate + H2O | phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 | Bifidobacterium pseudocatenulatum ATCC 27919 | 1D-myo-inositol pentakisphosphate + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | ? | x * 68000, recombinant enzyme, SDS-PAGE | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | ? | x * 68000, recombinant enzyme, SDS-PAGE | Bifidobacterium pseudocatenulatum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | BIFPSEUDO_03792 | - |
Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | Blon_0263 | - |
Bifidobacterium longum subsp. infantis |
| 3.1.3.8 | More | cf. EC 3.1.3.26 | Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | More | cf. EC 3.1.3.26 | Bifidobacterium longum subsp. infantis |
| 3.1.3.8 | phytase | - |
Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | phytase | - |
Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | BIFPSEUDO_03792 | - |
Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | Blon_0263 | - |
Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | More | cf. EC 3.1.3.8 | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | More | cf. EC 3.1.3.8 | Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | phytase | - |
Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | phytase | - |
Bifidobacterium longum subsp. infantis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 50 | - |
assay at | Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | 50 | - |
assay at | Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | 50 | - |
assay at | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | 50 | - |
assay at | Bifidobacterium longum subsp. infantis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 5.5 | - |
assay at | Bifidobacterium pseudocatenulatum |
| 3.1.3.8 | 5.5 | - |
assay at | Bifidobacterium longum subsp. infantis |
| 3.1.3.26 | 5.5 | - |
assay at | Bifidobacterium pseudocatenulatum |
| 3.1.3.26 | 5.5 | - |
assay at | Bifidobacterium longum subsp. infantis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
