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Literature summary for 3.2.1.81 extracted from
- Enhancing the thermostability of a novel beta-agarase AgaB through directed evolution (2008), Appl. Biochem. Biotechnol., 151, 51-59.
Application
| Application | Comment | Organism |
|---|---|---|
| industry | creation of a thermostable mutant L122Q/N446I of beta-agarase AgaB by directed evolution. The higher thermostability of mutant L122Q/N446I, in conjunction with its high specific activity and product specificity, will allow this enzyme to have potentials in industrial applications | Pseudoalteromonas sp. CY24 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| mutants cloned into vector pET-24a (+) and expressed in Escherichia coli BL21 (DE3). Expression of the agaB gene in vector pBS-ks(sv) and transformed to the Escherichia coli DH5alpha strain | Pseudoalteromonas sp. CY24 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L122Q | shows similar thermostability with wild-type AgaB, raises specific activity 1.3fold | Pseudoalteromonas sp. CY24 |
| L122Q/N446I | has higher thermostability and slightly increased specific activity (1.1fold) than wild-type AgaB. Melting temperature of S2 is 4.6°C higher than that of wild-type AgaB, and the half-life of S2 is 350 min at 40°C, which is 18.4fold longer than that of the wild-type enzyme. Comparable pH stability and optimum pH and temperature profiles as the wild-type | Pseudoalteromonas sp. CY24 |
| N446I | has similar enhanced thermostability as mutant L122Q/N446I, and decreased specific activity by 10-20% as compared to the wild-type | Pseudoalteromonas sp. CY24 |
| N446L | the half-life at 40°C is 12.9fold longer than that of wild-type AgaB | Pseudoalteromonas sp. CY24 |
| N446V | the half-life at 40°C is 18.2fold longer than that of wild-type AgaB | Pseudoalteromonas sp. CY24 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudoalteromonas sp. CY24 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant AgaB and mutants purified by ammonium sulfate precipitation, weak anion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. Mutant S2 purified about 476.5fold, with a final yield of 20.9% | Pseudoalteromonas sp. CY24 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AgaB | - |
Pseudoalteromonas sp. CY24 |
| agarase | - |
Pseudoalteromonas sp. CY24 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
mutant L122Q/N446I has comparable temperature profiles as the wild-type | Pseudoalteromonas sp. CY24 |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant L122Q/N446I has higher thermostability than wild-type AgaB. Melting temperature of S2 is 4.6°C higher than that of wild-type AgaB, and the half-life of mutant L122Q/N446I is 350 min at 40°C, which is 18.4fold longer than that of the wild-type enzyme. Mutant N446I has similar enhanced thermostability as mutant L122Q/N446I. L122Q shows similar thermostability with wild-type AgaB. Half-life of mutant N446V at 40°C is 18.2fold longer than that of wild-type AgaB. Half-life of mutant N446L at 40°C is 12.9fold longer than that of wild-type AgaB | Pseudoalteromonas sp. CY24 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant L122Q/N446I has comparable optimum pH as the wild-type | Pseudoalteromonas sp. CY24 |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
mutant L122Q/N446I has comparable pH stability as the wild-type | Pseudoalteromonas sp. CY24 |
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