EC Number   |
Application |
Reference |
|---|
   3.1.1.101 | analysis |
determination of enzymatic hydrolysis by measuring the change of intensity of transmitted light due to the scattering effect of PET nanoparticles immobilized in an agarose gel |
-, 738879 |
| 3.1.1.101 | analysis |
fluorimetric assay for the fast determination of the activity of polyester-hydrolyzing enzymes in a large number of samples. The assay is robust at different buffer concentrations, reaction times, pH values, and in the presence of proteins and can be used to quantify the amount of terephthalate obtained as the final degradation product of the enzymatic hydrolysis of PET in a microplate format |
-, 737919 |
| 3.1.1.101 | degradation |
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films |
-, 750147 |
| 3.1.1.101 | degradation |
a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa |
-, 737916 |
| 3.1.1.101 | degradation |
a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa. The dual enzyme system with LC-cutinase produces a 2.4fold higher amount of degradation products compared to Thermobifida fusca enzyme Cut2 after a reaction time of 24 h |
737916 |
| 3.1.1.101 | degradation |
at 50°C, a maximum hydrolysis rate for poly(ethylene terephthalate) nanoparticles of 0.0033 per min is determined with 80 microg/ml of Tcur_1278. With 50 microg/ml of Tcur_1278, the hydrolysis rate increases 1.8fold at 55°C and 2.6fold at 60°C |
-, 737423 |
| 3.1.1.101 | degradation |
at 50°C, a maximum hydrolysis rate of poly(ethylene terephthalate) nanoparticles of 0.0059 per min is determined with 20 microg/ml of Tcur_0390 |
-, 737423 |
| 3.1.1.101 | degradation |
bioconversion of plastics |
-, 751663 |
| 3.1.1.101 | degradation |
biodegradability of PET is mainly influenced by the mobility of the polyester chains, which determine the affinity and accessibility of the ester bonds to the enzyme. The hydrolysis rates of enzymatic PET degradation are predominantly controlled by the efficient substrate adsorption rather than by the hydrolysis of the ester bonds. Nanoparticles prepared from PET samples of different crystallinity show a high proportion of amorphous domains and thus in the corresponding biodegradability |
-, 738879 |
| 3.1.1.101 | degradation |
due to its low structural stability and solubility, it is difficult to apply standard laboratory-level Ideonella sakaiensis PETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. The extracellular enzyme is successfully produced using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. The secreted IsPETase has PET-degradation activity. The work will be used for development of a new Escherichia coli strain capable of degrading and assimilating PET in its culture medium |
-, 749827 |
