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Literature summary for 3.1.1.74 extracted from
- Cutinases: Properties and industrial applications (2009), Adv. Appl. Microbiol., 66, 77-95.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | water:surfactant molar rate has a marked influence on the enzyme activity, with the best results in the range between 5 and 8. The use of detergents improves the reaction yield during wetting of cotton fibers. Increase in the stereoselectivity of the primary hydroxyl group acylation is obtained through the preincubation of the enzyme in the presence of the substrate diol 1, there is no correlation with the incubation time | Fusarium solani |
Application
| Application | Comment | Organism |
|---|---|---|
| industry | useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions | Humicola insolens |
| industry | useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions | Fusarium oxysporum |
| industry | useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Cutinase proves to be the most well fitted enzyme for the detection of pesticide residues in foods even at very low levels. Use in fiber modification due to its hydrophobic nature and activity against biopolyesters present in plant cuticle. Use of cutinase to improve the wetting of cotton fibers. Cutinase is potentially useful for the removal of fats in laundry, but the unfolding of the enzyme in the presence of anionic surfactants limits its widespread use as an additive in industrial laundry detergents. Displays a stability profile that is well-fitted to the industrial process | Fusarium solani |
| industry | useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process | Humicola insolens |
| industry | useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process | Aspergillus oryzae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Fusarium solani |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | because the organism has a low but significant FAE activity, it may be easier to introduce a high level of FAE activity in cutinases through point mutations | Humicola insolens |
| additional information | because the organism has a low but significant FAE activity, it may be easier to introduce a high level of FAE activity in cutinases through point mutations | Aspergillus oryzae |
| additional information | stability of cutinase may be increased through mutations designed to avoid the transient formation of hydrophobic groups during protein movement. Because the organism has a low but significant ferulic acid esterase activity, it may be easier to introduce a high level of ferulic acid esterase activity in cutinases through point mutations | Fusarium solani |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | inhibition by organophosphate pesticides. Carbamate pesticides reveal an efficient cutinase inhibitor effect, though less potent than the organophosphates | Fusarium solani |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| additional information | hexanol has a stabilizing effect on the enzyme activity in reverse micelles | Fusarium solani |
| vinyl acetate | has a stabilizing effect on the enzyme activity | Fusarium solani |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
| Fusarium oxysporum | - |
- |
- |
| Fusarium solani | - |
pisi | - |
| Humicola insolens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihexylphthalate + H2O | degradation by cutinase is nearly 70% after 4 h, while 85% of the initial amount remains intact after 72 h of incubation with Candida cylindracea esterase. Products of cutinase-catalyzed hydrolysis are less toxic than those employing Candida cylindracea esterase | Fusarium oxysporum | ? | - |
? |  |
| malathion + H2O | - |
Fusarium oxysporum | ? | - |
? | |
| additional information | shows promising activity in polymerization reactions | Humicola insolens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cutin hydrolase | - |
Humicola insolens |
| cutin hydrolase | - |
Aspergillus oryzae |
| cutin hydrolase | - |
Fusarium solani |
| cutin hydrolase | - |
Fusarium oxysporum |
| cutinase | - |
Humicola insolens |
| cutinase | - |
Aspergillus oryzae |
| cutinase | - |
Fusarium solani |
| cutinase | - |
Fusarium oxysporum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 50 | - |
Fusarium solani |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
presence of hexanol and the low water content lead to the enzyme stabilization in the interior of the micelles, increasing its thermostability | Fusarium solani |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9 | has activity superior to lipases | Humicola insolens |
| 5 | 9 | has activity superior to lipases | Aspergillus oryzae |
| 5 | 9 | has activity superior to lipases | Fusarium solani |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | cutinases are hydrolytic enzymes that share properties of lipases and esterases, and also display the unique characteristic of being active regardless of the presence of an interface | Fusarium solani |
| physiological function | cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are active regardless of the presence of an interface | Humicola insolens |
| physiological function | cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are active regardless of the presence of an interface | Aspergillus oryzae |
| physiological function | cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are active regardless of the presence of an interface | Fusarium oxysporum |
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