Application | Comment | Organism |
---|---|---|
industry | the enzyme is mainly utilized in textile industry | Thermobifida fusca |
Cloned (Comment) | Organism |
---|---|
recombinant expression via type II secretory system in Escherichia coli strain BL21(DE3), the protein accumulates in the periplasmic space. The alpha-hemolysin secretion system can export target proteins directly from cytoplasm across both cell membrane of Escherichia coli to the culture medium and is therefore used for expression of the extracellular enzyme, method optimization for large-scale industrial production, overview | Thermobifida fusca |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Thermobifida fusca | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Thermobifida fusca | cutinase is a multi-functional esterase, which shows hydrolytic activity (cutin and a variety of soluble synthetic esters, insoluble triglycerides and polyesters), synthetic activity and transester activity | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermobifida fusca | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant extracellular enzyme 2.0fold from culture supernatant by ammonium sulfate precipitation and two different steps of anion exchange chromatography | Thermobifida fusca |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
446.2 | - |
purified recombinant alpha-hemolysin-enzyme, substrate 4-nitrophenyl butyrate, pH 8.0, 50°C | Thermobifida fusca |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl butyrate + H2O | - |
Thermobifida fusca | 4-nitrophenol + butyrate | - |
? | |
cutin + H2O | - |
Thermobifida fusca | cutin monomers | reaction products include hexadecanoic acid, octadecanoic acid, 9-octadecenoic acid, 9,12-octadecadienoic acid, 16-hydroxy hexadecanoic acid, and 18-hydroxyoctadeca-9,12-dienoic acid, ratios of wild-type and recombinant alpha-hemolysin-enzyme differ, overview | ? | |
additional information | cutinase is a multi-functional esterase, which shows hydrolytic activity (cutin and a variety of soluble synthetic esters, insoluble triglycerides and polyesters), synthetic activity and transester activity | Thermobifida fusca | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
wild-type enzyme | Thermobifida fusca |
70 | - |
recombinant alpha-hemolysin-enzyme | Thermobifida fusca |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
purified recombinant alpha-hemolysin-cutinase retains more than 90% of its maximal activity after incubation at pH 4.0-11.0 for 24 h, which is superior to that of wild-type cutinase | Thermobifida fusca |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
recombinant alpha-hemolysin-enzyme | Thermobifida fusca |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 11 | purified recombinant alpha-hemolysin-cutinase retains more than 90% of its maximal activity after incubation at 37°C for 24 h in this pH range, which is superior to that of wild-type cutinase | Thermobifida fusca |