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Literature summary for 4.2.1.1 extracted from

  • Sharma, A.; Bhattacharya, A.
    Enhanced biomimetic sequestration of CO2 into CaCO3 using purified carbonic anhydrase from indigenous bacterial strains (2010), J. Mol. Catal. B, 67, 122-128.
No PubMed abstract available

Application

Application Comment Organism
environmental protection the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst Bos taurus
environmental protection the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst Micrococcus luteus
environmental protection the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst Pseudomonas fragi
environmental protection the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst Micrococcus lylae

Inhibitors

Inhibitors Comment Organism Structure
As3+
-
Bos taurus
As3+
-
Micrococcus luteus
As3+
-
Micrococcus lylae
As3+
-
Pseudomonas fragi
bicarbonate
-
Bos taurus
bicarbonate
-
Micrococcus luteus
bicarbonate
-
Micrococcus lylae
bicarbonate
-
Pseudomonas fragi
bromide
-
Micrococcus luteus
bromide
-
Micrococcus lylae
bromide
-
Pseudomonas fragi
Ca2+ 25% inhibition at 0.2 mM Bos taurus
Ca2+ 25% inhibition at 0.2 mM Micrococcus luteus
Ca2+ 25% inhibition at 0.2 mM Micrococcus lylae
Ca2+ 25% inhibition at 0.2 mM Pseudomonas fragi
chloride
-
Bos taurus
chloride
-
Micrococcus luteus
chloride
-
Micrococcus lylae
chloride
-
Pseudomonas fragi
Hg2+
-
Bos taurus
Hg2+
-
Micrococcus luteus
Hg2+
-
Micrococcus lylae
Hg2+
-
Pseudomonas fragi
Iodide
-
Micrococcus luteus
Iodide
-
Micrococcus lylae
Iodide
-
Pseudomonas fragi
K+ 25% inhibition at 0.2 mM Bos taurus
K+ 25% inhibition at 0.2 mM Micrococcus luteus
K+ 25% inhibition at 0.2 mM Micrococcus lylae
K+ 25% inhibition at 0.2 mM Pseudomonas fragi
Mg2+ 25% inhibition at 0.2 mM Bos taurus
Mg2+ 25% inhibition at 0.2 mM Micrococcus luteus
Mg2+ 25% inhibition at 0.2 mM Micrococcus lylae
Mg2+ 25% inhibition at 0.2 mM Pseudomonas fragi
Na+ 25% inhibition at 0.2 mM Bos taurus
Na+ 25% inhibition at 0.2 mM Micrococcus luteus
Na+ 25% inhibition at 0.2 mM Micrococcus lylae
Na+ 25% inhibition at 0.2 mM Pseudomonas fragi
nitrate
-
Bos taurus
nitrate
-
Micrococcus luteus
nitrate
-
Micrococcus lylae
nitrate
-
Pseudomonas fragi
Pb2+
-
Bos taurus
Pb2+
-
Micrococcus luteus
Pb2+
-
Micrococcus lylae
Pb2+
-
Pseudomonas fragi
sulfate
-
Bos taurus
sulfate
-
Micrococcus luteus
sulfate
-
Micrococcus lylae
sulfate
-
Pseudomonas fragi

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Micrococcus luteus
-
-
-
Micrococcus luteus 2
-
-
-
Micrococcus lylae
-
-
-
Pseudomonas fragi
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
61
-
purified enzyme, pH 8.3, 4°C Micrococcus luteus
66.5
-
purified enzyme, pH 8.3, 4°C Micrococcus lylae
70.6
-
purified enzyme, pH 8.3, 4°C Pseudomonas fragi
74.6
-
purified enzyme, pH 8.3, 4°C Bos taurus

Synonyms

Synonyms Comment Organism
carbonic anhydrase
-
Bos taurus
carbonic anhydrase
-
Micrococcus luteus
carbonic anhydrase
-
Pseudomonas fragi
carbonic anhydrase
-
Micrococcus lylae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4
-
assay at Bos taurus
4
-
assay at Micrococcus luteus
4
-
assay at Pseudomonas fragi
4
-
assay at Micrococcus lylae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview Bos taurus
additional information
-
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview Micrococcus luteus
additional information
-
effect of pH and temperature as function of time on stability of CAs from different species, overview Pseudomonas fragi
additional information
-
the enzyme exhibits more than 80% stability between pH 7.0 and pH 8.0, while 68% and 57% are retained at pH 8.5 and pH 9.0 after 3 h of incubation. The enzyme retains 63%, 54% and 45% residual activity at pH 8.0, pH 8.5, and pH 9.0, respectively, following 6 h of incubation. Effect of pH and temperature as function of time on stability of CAs from different species, overview Micrococcus lylae
35 45 the purifed enzyme retains 38-54% after 6 h Bos taurus
35 45 the purifed enzyme retains 40-51% after 6 h Micrococcus lylae
35 45 the purifed enzyme retains 65-50% after 6 h Pseudomonas fragi
35 45 the purifed enzyme retains 71-83% after 6 h Micrococcus luteus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
assay at Bos taurus
8.3
-
assay at Micrococcus luteus
8.3
-
assay at Pseudomonas fragi
8.3
-
assay at Micrococcus lylae

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
42%, 39% and 36% stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively for commercial bovine carbonic anhydrase following 6 h of incubation. After 3 h incubation at pH 7.0 and pH 7.5, bovin retains 81% and 75% residual activity, while 79%, 69%, 61%, stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively. Effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview Bos taurus
additional information
-
effect of pH and temperature as function of time on stability of CAs from different species, overview Micrococcus lylae
additional information
-
the enzyme shows 78% stability along with 71% and 73% residual activity at pH 8.0 and pH 9.0, respectively, following 6 h of incubation, after 3 h of incubation 80% stability is observed between pH 7.5-9.0, effect of pH and temperature as function of time on stability of CAs from different species, overview Micrococcus luteus
7 9 the enzyme retains 88% residual activity at pH 8.0, 72% residual activity at pH 8.5, and 66% residual activity at pH 9.0 following 6 h of incubation, stable at 80% of maximal activity in the pH range pH 7.0-9.0 following 3 h of incubation, effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview Pseudomonas fragi

General Information

General Information Comment Organism
additional information evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase Bos taurus
additional information evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase Micrococcus luteus
additional information Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA Pseudomonas fragi
additional information Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA Micrococcus lylae