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(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
(ethylene terephthalate)n + H2O
terephthalic acid + mono(2-hydroxyethyl)terephthalate + ?
hydrolysis of poly(ethylene terephthalate) (PET) is shown for all three enzymes (native Thc_Cut1 and two glycosylation site knockout mutants (Thc_Cut1_koAsn and Thc_Cut1_koST)) based on quantification of released products by HPLC and similar concentrations of released terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET)
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
3-hydroxybutyric acid + ?
polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
polyesters poly(butylene succinate) + H2O
succinic acid + 1,4-butanediol + ?
polyesters poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
polyethylene-2,5-furandicarboxylate + H2O
?
additional information
?
-
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
-
-
-
?
(epsilon-caprolactone)n + H2O
(epsilon-caprolactame)n-1 + ethylene terephthalate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
high flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
substrates are amorphous PET film or PET fibers
terephthalate is the dominant hydrolysis product detected after a reaction time of 50 h at 65°C. Monohydroxyethylene terephthalate which inhibits the hydrolysis of PET is almost completely converted into terephthalate and accounts for less than 9.1% of the total hydrolysis products
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
substrates are amorphous PET film or PET fibers
terephthalate is the dominant hydrolysis product detected after a reaction time of 50 h at 65°C. Monohydroxyethylene terephthalate which inhibits the hydrolysis of PET is almost completely converted into terephthalate and accounts for less than 9.1% of the total hydrolysis products
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
E5BBQ3
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + 4-[(2-hydroxyethoxy)carbonyl]benzoate
-
4-[(2-hydroxyethoxy)carbonyl]benzoate is the predominant product
-
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
-
mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
-
?
(ethylene terephthalate)n + H2O
(ethylene terephthalate)n-1 + mono(2-hydroxyethyl)terephthalic acid
-
mono(2-hydroxyethyl)terephthalic acid is the major product, plus minor amounts of terephthalic acid and bis(2-hydroxyethyl) terephthalic acid
-
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
-
-
-
?
4-nitrophenyl acetate + H2O
acetate + 4-nitrophenol
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
-
enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
-
?
bis(2-hydroxyethyl) terephthalic acid + H2O
mono(2-hydroxyethyl)terephthalic acid + ethylene glycol
-
enzyme does not catalyze further decomposition of mono(2-hydroxyethyl)terephthalic acid
-
?
polyethylene-2,5-furandicarboxylate + H2O
?
-
-
-
?
polyethylene-2,5-furandicarboxylate + H2O
?
-
-
-
?
additional information
?
-
enzyme shows low activity on 4-nitrophenyl aliphatic esters
-
-
?
additional information
?
-
enzyme shows low activity on 4-nitrophenyl aliphatic esters
-
-
?
additional information
?
-
E5BBQ3
analysis of the partially hydrolyzed PET nanoparticles provides indirect evidence for an endo-type hydrolytic mechanism of Cut2 in the heterogeneous degradation of aromatic polyesters
-
-
?
additional information
?
-
E5BBQ3
enzyme additionally catalyzes hydrolysis of ethylene terephthalate and bis(2-hydroxyethyl) terephthalic acid, reaction of EC 3.1.1.102
-
-
?
additional information
?
-
E5BBQ3
analysis of the partially hydrolyzed PET nanoparticles provides indirect evidence for an endo-type hydrolytic mechanism of Cut2 in the heterogeneous degradation of aromatic polyesters
-
-
?
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A180I
mutation results in more space on the binding center and higher activity than the wild-type enzyme
C174S
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
C210S
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is is abolished
D177A
inactive mutant enzyme
H208A
inactive mutant enzyme
I179A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
I179F
-
enzymatic activity of the mutant enzyme exhibits 2.5fold increase in comparison with wild-type PETase
L88F
-
enzymatic activity of the mutant enzyme exhibits 2.1fold increase in comparison with wild-type PETase
Q90A
marked decrease in hydrolysis activity
R61A
-
enzymatic activity of the mutant enzyme exhibits 1.4fold increase in comparison with wild-type PETase
S185H
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 45% compared to wild-type value
S209F
strongly reduced hydrolysis of the PET particles
S238F/W159H
the mutant enzyme adopts a more productive interaction with PET
T59A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 95% compared to wild-type value
C174S
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
-
C210S
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is is abolished
-
D177A
-
inactive mutant enzyme
-
H208A
-
inactive mutant enzyme
-
S238F/W159H
-
the mutant enzyme adopts a more productive interaction with PET
-
T59A
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 95% compared to wild-type value
-
Y58A
-
mutation results in more space on the binding center and higher activity than the wild-type enzyme
-
D174C/D253C
E5BBQ3
increase in melting temperature in absence and in presence of Ca2+
D204C/E253C
E5BBQ3
increase in melting temperature
D204C/E253C/D174R
E5BBQ3
increase in temperature optimum to 75-80°C, mutant causes a weight loss of PET films of 25.0% at 70 °C after a reaction time of 48 h, compared to 0.3% for wild-type
D204R
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
E253R
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
D174C/D253C
-
increase in melting temperature in absence and in presence of Ca2+
-
D204C/E253C
-
increase in melting temperature
-
D204C/E253C/D174R
-
increase in temperature optimum to 75-80°C, mutant causes a weight loss of PET films of 25.0% at 70 °C after a reaction time of 48 h, compared to 0.3% for wild-type
-
D204R
-
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
-
E253R
-
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point
-
M132A
marked decrease in hydrolysis activity
M132A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
S131A
inactive mutant enzyme
S131A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value
W130A
mutation results in more space on the binding center and higher activity than the wild-type enzyme
W130A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
W130H
mutation results in more space on the binding center and higher activity than the wild-type enzyme
W130H
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
W156A
marked decrease in hydrolysis activity
W156A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
Y58A
mutation results in more space on the binding center and higher activity than the wild-type enzyme
Y58A
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 80% compared towild-type value
W130A
-
mutation results in more space on the binding center and higher activity than the wild-type enzyme
-
W130A
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 15% compared to wild-type value
-
W156A
-
marked decrease in hydrolysis activity
-
W156A
-
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to about 10% compared to wild-type value
-
G62A
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Mutant G62A reveals a 5.5fold lower binding constant to the inhibitor mono-(2-hydroxyethyl) terephthalate than the wild type enzyme
G62A
E5BBQ3
mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Kinetic analysis based on the released PET hydrolysis products confirms the superior hydrolytic activity of G62A with a fourfold higher hydrolysis rate constant and a 1.5fold lower substrate binding constant than those of the wild type enzyme. Mutant enzyme G62A reveals a 5.5fold lower binding constant to the inhibitor than the wild type enzyme indicating that its increased PET hydrolysis activity is the result of a relieved product inhibition by mono-(2-hydroxyethyl) terephthalate
G62A/I213S
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
G62A/I213S
E5BBQ3
mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
G62A
-
mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Kinetic analysis based on the released PET hydrolysis products confirms the superior hydrolytic activity of G62A with a fourfold higher hydrolysis rate constant and a 1.5fold lower substrate binding constant than those of the wild type enzyme. Mutant enzyme G62A reveals a 5.5fold lower binding constant to the inhibitor than the wild type enzyme indicating that its increased PET hydrolysis activity is the result of a relieved product inhibition by mono-(2-hydroxyethyl) terephthalate
-
G62A
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Mutant G62A reveals a 5.5fold lower binding constant to the inhibitor mono-(2-hydroxyethyl) terephthalate than the wild type enzyme
-
G62A/I213S
-
mutant enzyme shows highly increased activity in hydrolyzing PET films and fibers. The mutant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
-
G62A/I213S
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
-
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analysis
E5BBQ3
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
analysis
E5BBQ3
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
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
-
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
-
degradation
E5BBQ3
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
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
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
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
degradation
E5BBQ3
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
degradation
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures
degradation
E5BBQ3
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
degradation
E5BBQ3
mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type
degradation
the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h
degradation
E5BBQ3
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
degradation
bioconversion of plastics
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
degradation
enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants
degradation
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
degradation
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
degradation
-
the enzyme is a potential tool to solve the issue of polyester plastic pollution
degradation
-
the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h
-
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
-
degradation
-
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme
-
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
-
degradation
-
mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type
-
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
-
degradation
-
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures
-
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
-
degradation
-
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
-
degradation
-
enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants
-
degradation
-
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
-
degradation
-
bioconversion of plastics
-
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
-
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
-
environmental protection
E5BBQ3
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
environmental protection
bioconversion of plastics
environmental protection
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
environmental protection
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
environmental protection
-
the enzyme is a potential tool to solve the issue of polyester plastic pollution
environmental protection
the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature
environmental protection
-
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
-
environmental protection
-
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry
-
environmental protection
-
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase)
-
environmental protection
-
bioconversion of plastics
-
environmental protection
-
the investigation of structure/function relationships can be used to guide further protein engineering to more effectively depolymerize PET and other synthetic polymers, thus informing a biotechnological strategy to help remediate the environmental scourge of plastic accumulation in nature
-
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Wei, R.; Oeser, T.; Then, J.; Khn, N.; Barth, M.; Schmidt, J.; Zimmermann, W.
Functional characterization and structural modeling of synthetic polyester-degrading hydrolases from Thermomonospora curvata
AMB Express
4
1-10
2014
Thermomonospora curvata (D1A2H1), Thermomonospora curvata (D1A9G5), Thermomonospora curvata DSM 43183 (D1A2H1), Thermomonospora curvata DSM 43183 (D1A9G5)
brenda
Roth, C.; Wei, R.; Oeser, T.; Then, J.; Foellner, C.; Zimmermann, W.; Straeter, N.
Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca
Appl. Microbiol. Biotechnol.
98
7815-7823
2014
Thermobifida fusca (E5BBQ3), Thermobifida fusca
brenda
Barth, M.; Oeser, T.; Wei, R.; Then, J.; Schmidt, J.; Zimmermann, W.
Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca
Biochem. Eng. J.
93
222-228
2015
Thermobifida fusca (E5BBQ3)
-
brenda
Wei, R.; Oeser, T.; Schmidt, J.; Meier, R.; Barth, M.; Then, J.; Zimmermann, W.
Engineered bacterial polyester hydrolases efficiently degrade polyethylene terephthalate due to relieved product inhibition
Biotechnol. Bioeng.
113
1658-1665
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Then, J.; Wei, R.; Oeser, T.; Barth, M.; Belisario-Ferrari, M.R.; Schmidt, J.; Zimmermann, W.
Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca
Biotechnol. J.
10
592-598
2015
Thermobifida fusca (E5BBQ2), Thermobifida fusca (E5BBQ3), Thermobifida fusca, Thermobifida fusca KW3 (E5BBQ2), Thermobifida fusca KW3 (E5BBQ3)
brenda
Barth, M.; Honak, A.; Oeser, T.; Wei, R.; Belisario-Ferrari, M.R.; Then, J.; Schmidt, J.; Zimmermann, W.
A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films
Biotechnol. J.
11
1082-1087
2016
Thermobifida fusca (E5BBQ3), uncultured bacterium (G9BY57), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Nimchua, T.; Punnapayak, H.; Zimmermann, W.
Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi
Biotechnol. J.
2
361-364
2007
Fusarium oxysporum, Fusarium vanettenii, Fusarium vanettenii DSM 62420, Fusarium oxysporum LCH I
brenda
Wei, R.; Oeser, T.; Billig, S.; Zimmermann, W.
A high-throughput assay for enzymatic polyester hydrolysis activity by fluorimetric detection
Biotechnol. J.
7
1517-1521
2012
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
brenda
Then, J.; Wei, R.; Oeser, T.; Gerdts, A.; Schmidt, J.; Barth, M.; Zimmermann, W.
A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate
FEBS open bio
6
425-432
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
brenda
Schmidt, J.; Wei, R.; Oeser, T.; Belisario-Ferrari, M.R.; Barth, M.; Then, J.; Zimmermann, W.
Effect of Tris, MOPS, and phosphate buffers on the hydrolysis of polyethylene terephthalate films by polyester hydrolases
FEBS open bio
6
919-927
2016
Thermobifida fusca (E5BBQ3), uncultured bacterium (G9BY57), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Wei, R.; Oeser, T.; Barth, M.; Weigl, N.; Lbs, A.; Schulz-Siegmund, M.; Hacker, M.; Zimmermann, W.
Turbidimetric analysis of the enzymatic hydrolysis of polyethylene terephthalate nanoparticles
J. Mol. Catal. B
103
72-78
2014
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3)
-
brenda
Yoshida, S.; Hiraga, K.; Takehana, T.; Taniguchi, I.; Yamaji, H.; Maeda, Y.; Toyohara, K.; Miyamoto, K.; Kimura, Y.; Oda, K.
A bacterium that degrades and assimilates poly(ethylene terephthalate)
Science
351
1196-1199
2016
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Danso, D.; Schmeisser, C.; Chow, J.; Zimmermann, W.; Wei, R.; Leggewie, C.; Li, X.; Hazen, T.; Streit, W.R.
New insights into the function and global distribution of polyethylene terephthalate (PET)-degrading bacteria and enzymes in marine and terrestrial metagenomes
Appl. Environ. Microbiol.
84
e02773-17
2018
Ideonella sakaiensis (A0A0K8P6T7), uncultured bacterium (C3RYL0), uncultured bacterium (G9BY57), Thermomonospora curvata (D1A9G5), Thermobifida fusca (E5BBQ3), Thermobifida fusca (E9LVI0), Thermobifida alba (E9LVH7), Thermobifida cellulosilytica (E9LVH9), Thermobifida halotolerans (H6WX58), Saccharomonospora viridis (W0TJ64), Thermomonospora curvata DSM 43183 (D1A9G5)
brenda
Seo, H.; Kim, S.; Son, H.F.; Sagong, H.Y.; Joo, S.; Kim, K.J.
Production of extracellular PETase from Ideonella sakaiensis using sec-dependent signal peptides in E. coli
Biochem. Biophys. Res. Commun.
508
250-255
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7), Ideonella sakaiensis 201-F6
brenda
Fecker, T.; Galaz-Davison, P.; Engelberger, F.; Narui, Y.; Sotomayor, M.; Parra, L.P.; Ramirez-Sarmiento, C.A.
Active site flexibility as a hallmark for efficient PET degradation by I. sakaiensis PETase
Biophys. J.
114
1302-1312
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Wei, R.; Oeser, T.; Schmidt, J.; Meier, R.; Barth, M.; Then, J.; Zimmermann, W.
Engineered bacterial polyester hydrolases efficiently degrade polyethylene terephthalate due to relieved product inhibition
Biotechnol. Bioeng.
113
1658-1665
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Barth, M.; Honak, A.; Oeser, T.; Wei, R.; Belisario-Ferrari, M.R.; Then, J.; Schmidt, J.; Zimmermann, W.
A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films
Biotechnol. J.
11
1082-1087
2016
Thermobifida fusca (E5BBQ3), Thermobifida fusca KW3 (E5BBQ3), Thermobifida fusca KW3
brenda
Liu, B.; He, L.; Wang, L.; Li, T.; Li, C.; Liu, H.; Luo, Y.; Bao, R.
Protein crystallography and site-direct mutagenesis analysis of the poly(ethylene terephthalate) hydrolase PETase from Ideonella sakaiensis
ChemBioChem
19
1471-1475
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Furukawa, M.; Kawakami, N.; Oda, K.; Miyamoto, K.
Acceleration of enzymatic degradation of poly(ethylene terephthalate) by surface coating with anionic surfactants
ChemSusChem
11
4018-4025
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Ma, Y.; Yao, M.; Li, B.; Ding, M.; He, B.; Chen, S.; Zhou, X.; Yuan, Y.
Enhanced poly(ethylene terephthalate) hydrolase activity by protein engineering
Engineering
4
888-893
2018
Ideonella sakaiensis
-
brenda
Chen, C.C.; Han, X.; Ko, T.P.; Liu, W.; Guo, R.T.
Structural studies reveal the molecular mechanism of PETase
FEBS J.
285
3717-3723
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Gamerith, C.; Vastano, M.; Ghorbanpour, S.M.; Zitzenbacher, S.; Ribitsch, D.; Zumstein, M.T.; Sander, M.; Herrero Acero, E.; Pellis, A.; Guebitz, G.M.
Enzymatic degradation of aromatic and aliphatic polyesters by P. pastoris expressed cutinase 1 from Thermobifida cellulosilytica
Front. Microbiol.
8
938
2017
Thermobifida cellulosilytica (E9LVH8)
brenda
Huang, X.; Cao, L.; Qin, Z.; Li, S.; Kong, W.; Liu, Y.
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide
J. Agric. Food Chem.
66
13217-13227
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
de Castro, A.M.; Carniel, A.; Nicomedes Junior, J.; da Conceicao Gomes, A.; Valoni, E.
Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources
J. Ind. Microbiol. Biotechnol.
44
835-844
2017
Aspergillus oryzae, Burkholderia cepacia, Moesziomyces antarcticus, Diutina rugosa, Humicola insolens, Thermomyces lanuginosus, Rhizomucor miehei, Pseudomonas fluorescens, Rhizopus arrhizus, Rhizopus niveus, Sus scrofa, Triticum aestivum
brenda
Han, X.; Liu, W.; Huang, J.W.; Ma, J.; Zheng, Y.; Ko, T.P.; Xu, L.; Cheng, Y.S.; Chen, C.C.; Guo, R.T.
Structural insight into catalytic mechanism of PET hydrolase
Nat. Commun.
8
2106
2017
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis, Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Joo, S.; Cho, I.; Seo, H.; Son, H.; Sagong, H.; Shin, T.; Choi, S.; Lee, S.; Kim, K.
Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
Nat. Commun.
9
382
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis 201-F6 (A0A0K8P6T7)
brenda
Austin, H.P.; Allen, M.D.; Donohoe, B.S.; Rorrer, N.A.; Kearns, F.L.; Silveira, R.L.; Pollard, B.C.; Dominick, G.; Duman, R.; El Omari, K.; Mykhaylyk, V.; Wagner, A.; Michener, W.E.; Amore, A.; Skaf, M.S.; Crowley, M.F.; Thorne, A.W.; Johnson, C.W.; Woodcock, H.L.; McGeehan, J.E.; Beckham, G.T.
Characterization and engineering of a plastic-degrading aromatic polyesterase
Proc. Natl. Acad. Sci. USA
115
E4350-E4357
2018
Ideonella sakaiensis (A0A0K8P6T7), Ideonella sakaiensis 201-F6 (A0A0K8P6T7), Ideonella sakaiensis 201-F6
brenda