Any feedback?
Literature summary extracted from
- Practical application of different enzymes immobilized on sepabeads (2008), Bioprocess Biosyst. Eng., 31, 163-171.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.1.3 | biotechnology | biocatalytic surfactant production, for example the synthesis of myristyl myristate. | Moesziomyces antarcticus |
| 3.2.1.4 | biotechnology | Production of immobilized enzyme on Sepabeads EC-BU (hydrophobic interactions are the driving force for the adsorption of the enzyme to the carrier) | Pseudomonas putida |
| 4.1.1.7 | biotechnology | Production of immobilized enzyme on Sepabeads EC-EA by C-C coupling | Pseudomonas putida |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.4 | The gene encoding for the thermoactive endoglucanase is derived from a metagenomic gene library based on a mixed culture grown anaerobically on cellulose at 70 C and pH 7. The recombinant endoglucanase is actively expressed in Escherichia coli TunerTM(DE3)pLacI by induction with 1 mM IPTG. | Pseudomonas putida |
| 4.1.1.7 | Production as hexahistidine fusion protein by fermentation of Escherichia coli cells as host strain. | Pseudomonas putida |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.1.1.3 | The stability of Sepabeads EC-EP-CALB is investigated within the solvent-free system polyglycerol+lauric acid. The limiting factor of this system is its high viscosity and the different polarities of the starting materials. This causes a two phase system, whereby the detergent form formed as a product accounts for some leaching of the biocatalyst. These are challenges for the optimized use of the prepared biocatalyst. Using it in a repetitive batch mode gives information about the stability in the esterification reaction. The initial reaction rate is found to be 500 U/g and decreases within eight batches to 130 U/g. | Moesziomyces antarcticus |
| 4.1.1.7 | The freeze-drying of immobilized Sepabeads EC-EA/BFD leads to an inactivation of the enzyme. | Pseudomonas putida |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.7 | Mg2+ | essential for the activity | Pseudomonas putida |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.3 | 33000 | - |
- |
Moesziomyces antarcticus |
| 3.2.1.4 | 85000 | - |
- |
Pseudomonas putida |
| 4.1.1.7 | 240000 | - |
- |
Pseudomonas putida |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.3 | additional information | Moesziomyces antarcticus | The conversion of the lauric acid is at 80% after 4 h whereas the residual amount of polyglycerol is at 50% at this time. The conversion of polyglycerol remains lower than the conversion of lauric acid, because of the multiple hydroxy functions within the mixture of different glycerol oligomers. The equilibrium of the reaction can be shifted to total conversion by removal of water applying vacuum to the stirred tank reactor. | ? | - |
? | |
| 3.1.1.3 | additional information | Moesziomyces antarcticus | The synthesis of myristyl myristate by Sepabeads EC-EP/CALB is an example for a biocatalytic surfactant production. | ? | - |
? | |
| 3.2.1.4 | additional information | Pseudomonas putida | beta-1,4-endoglucanases show activities of the cleavage of the cellulose backbone due to an endocleavage. Oligosaccharides of different lengths as well as cellobiose and glucose are formed | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.3 | Moesziomyces antarcticus | - |
- |
- |
| 3.2.1.4 | Pseudomonas putida | - |
- |
- |
| 4.1.1.7 | Pseudomonas putida | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.4 | by Ni-NTA column purification and pretreatment by heat denaturation to remove accompanying proteins | Pseudomonas putida |
| 4.1.1.7 | by Ni-NTA column purification. | Pseudomonas putida |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.1.3 | commercial preparation | Immobilization of CALB on Sepabeads EC-EP support | Moesziomyces antarcticus | - |
| 3.2.1.4 | cell culture | metagenome | Pseudomonas putida | - |
| 4.1.1.7 | cell culture | - |
Pseudomonas putida | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.3 | additional information | - |
Comparing the course of this reaction for myristyl myristate, to that catalyzed by Novozym 435, the biocatalyst Sepabeads EC-EP-CALB shows similar activity. | Moesziomyces antarcticus |
| 3.1.1.3 | additional information | - |
The CALB-Sepabeads EC-EP biocatalyst with an enzyme loading of 100 mg/g exhibits high activity towards the direct esterification of polyglycerol and lauric acid. | Moesziomyces antarcticus |
| 3.1.1.3 | additional information | - |
Using the immobilized lipase B, the synthesis of the bulk chemicals myristyl myristate and polyglycerol laurate can be carried out with an initial reaction rate of 0.40 and 1.24 kU/g. The corresponding half-life time is determined to be 12.9 hours. | Moesziomyces antarcticus |
| 4.1.1.7 | additional information | - |
After 24 h of catalytic activity the immobilized biocatalyst Sepabeads EC-EA/BFD showed a remaining activity of 5% of its initial value. | Pseudomonas putida |
| 4.1.1.7 | additional information | - |
specific activity of around 62 U/g dry carrier. The activity is determined for the reaction of acetaldehyde (500 mM) and benzaldehyde (50 mM) at pH 8.0 | Pseudomonas putida |
| 4.1.1.7 | additional information | - |
Stability of Sepabeads EC-EA/BFD is determined by repetitive batch experiments while carrying out the synthesis of 2-hydroxy-1-phenylpropanone. The reaction of benzaldehyde and acetaldehyde is carried out at 30°C and after each batch is washed. The decrease of the initial reaction rate is followed for six batches. The newly prepared biocatalyst (enzyme loading 320 mg/g) shows an initial reaction rate of 130 U/g carrier with respect to the C-C-coupling reaction, whereby the rate decreases down to 10% (13 U/g) in the sixth batch. | Pseudomonas putida |
| 4.1.1.7 | 11 | - |
activity of free BFD | Pseudomonas putida |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.3 | additional information | The conversion of the lauric acid is at 80% after 4 h whereas the residual amount of polyglycerol is at 50% at this time. The conversion of polyglycerol remains lower than the conversion of lauric acid, because of the multiple hydroxy functions within the mixture of different glycerol oligomers. The equilibrium of the reaction can be shifted to total conversion by removal of water applying vacuum to the stirred tank reactor. | Moesziomyces antarcticus | ? | - |
? | |
| 3.1.1.3 | additional information | The synthesis of myristyl myristate by Sepabeads EC-EP/CALB is an example for a biocatalytic surfactant production. | Moesziomyces antarcticus | ? | - |
? | |
| 3.2.1.4 | additional information | beta-1,4-endoglucanases show activities of the cleavage of the cellulose backbone due to an endocleavage. Oligosaccharides of different lengths as well as cellobiose and glucose are formed | Pseudomonas putida | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.3 | CALB | - |
Moesziomyces antarcticus |
| 3.1.1.3 | lipase B | - |
Moesziomyces antarcticus |
| 3.2.1.4 | endoglucanase | - |
Pseudomonas putida |
| 4.1.1.7 | benzoylformate decarboxylase | - |
Pseudomonas putida |
| 4.1.1.7 | BFD | - |
Pseudomonas putida |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 70 | - |
enzyme is thermoactive | Pseudomonas putida |
| 4.1.1.7 | 50 | - |
at pH 8.0 | Pseudomonas putida |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.7 | 20 | 70 | At temperatures above 70°C and lower than 20°C the activity decreases below 10 U/g carrier. | Pseudomonas putida |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | additional information | - |
free enzyme shows an activity of 75% of the initial activity after 30 min, and even an activity of 40% remained after 6 h, both measured at 70°C | Pseudomonas putida |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 6 | - |
- |
Pseudomonas putida |
| 4.1.1.7 | 8 | - |
assay at | Pseudomonas putida |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.7 | thiamine diphosphate | - |
Pseudomonas putida | |
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
