3.1.1.74: cutinase
This is an abbreviated version!
For detailed information about cutinase, go to the full flat file.
Word Map on EC 3.1.1.74
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3.1.1.74
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fusarium
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solani
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pi
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lipase
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terephthalate
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p-nitrophenyl
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lipolytic
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thermobifida
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esterases
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insolens
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fusca
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humicola
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ideonella
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polybutylene
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sakaiensis
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industry
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polycaprolactone
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tributyrin
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degradation
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sulfosuccinate
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haematococca
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monilinia
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terephthalic
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petase
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synthesis
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nectria
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hydrophobins
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saccharomonospora
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biotechnology
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environmental protection
- 3.1.1.74
- fusarium
- solani
- pi
- lipase
- terephthalate
- p-nitrophenyl
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lipolytic
- thermobifida
- esterases
- insolens
- fusca
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humicola
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ideonella
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polybutylene
- sakaiensis
- industry
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polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
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monilinia
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terephthalic
- petase
- synthesis
- nectria
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hydrophobins
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saccharomonospora
- biotechnology
- environmental protection
Reaction
Synonyms
acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489
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Application
Application on EC 3.1.1.74 - cutinase
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biotechnology
degradation
environmental protection
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application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible
industry
synthesis
additional information
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adsorption of enzyme onto the surface of poly(methyl methacrylate) latex particles. Up to 50% decrease in specific activity at pH-values 4.5 and 5.2. Almost no inactivation upon adsorption at pH 7.0 and 9.2. 60% increase in maximum adsorption with temperature raising from 25 to 50°C
biotechnology
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immobilization of enzyme on sodium form of zeolite Y, half-life 590 days at 30°C. Immobilization on zolite A, halft-life of 54 days at 30°C. Half-lives after immobilization on Alumina and Accurel-PA6 are 109 and 10 days, resp. Higher temperatures induce a remarkable stability loss in all preparations. At 30°C, enzymatic activities obtained wit the immobilization on zeolite A are the highest ones
biotechnology
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study on enzyme encapsulated in sol-gel matrices prepared with alkyl-alkoxysilane precursors of different chain length. Specific activity of entrapped enzyme is comparable to enzyme immobilized on zeolite Y, with incorporation of different additives bringing about an enhancement of enzyme activity and operational stability
biotechnology
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use of enzyme in a membrane reactor in presence of 1-hexanol, operational half-life of 674 days
biotechnology
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engineering new cutinase-inspired biocatalysts with tailor-made properties
biotechnology
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engineering new cutinase-inspired biocatalysts with tailor-made properties
biotechnology
high-level secretion of cutinase in Pichia pastoris may be a promising alternative to many expression systems previously used for the large-scale production of cutinase in Saccharomyces cerevisiae as well as Escherichia coli. The functional expression of a large amount of extracellular cutinase offers the opportunity for developing an efficient high-throughput screening procedure for the improvement of enzymatic property and the development of novel biocatalysis of cutinase
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efficient degradation of n-butyl benzyl phthalate by enzyme, degradation of 60% of initial amount within 7.5 h. Major product is 1,3-isobenzofurandione
degradation
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enzyme degrades 60% of initial 500 mg/l malathion within 0.5 h, major degradation product is malathion diacid
degradation
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enzyme shows significant degradation of dipropyl phthalate to non-toxic 1,3-isobenzofurandione, with 70% degradation of initial 500 mg/l within 2.5 h
degradation
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biotechnological applications of cutinases for synthetic polyester degradation
degradation
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biotechnological applications of cutinases for synthetic polyester degradation
degradation
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biotechnological applications of cutinases for synthetic polyester degradation
degradation
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biotechnological applications of cutinases for synthetic polyester degradation
degradation
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biotechnological applications of cutinases for synthetic polyester degradation
degradation
enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions
degradation
enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions
degradation
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enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions. It favors the hydrolysis of poly(ethyl acrylate) over poly(methyl acrylate)
degradation
enzyme is able to modify the surface of the polycaprolactone and polyethylene terephthalate synthetic polyesters
degradation
enzyme shows an ink removal efficiency of 78.4% on laser-printed paper and 81.3% on newspaper at 30°C
degradation
fusion of enzyme to the class II hydrophobins HFB4 and HFB7 or the pseudo-class I hydrophobin HFB9b. Upon fusion to HFB4 or HFB7, the hydrolysis of polyethylene terephthalate is enhanced over16fold over the level with the free enzyme
degradation
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surface hydrolysis of poly(ethylene terephthalate) fabric using recombinant cutinase. The optimal parameters are 40°C, pH 8, and 1.92 mg enzyme loading per gram of fabric
degradation
Thermothelomyces thermophilus DSM 1799
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enzyme shows an ink removal efficiency of 78.4% on laser-printed paper and 81.3% on newspaper at 30°C
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degradation
Aspergillus niger ATCC 10574
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enzyme is able to modify the surface of the polycaprolactone and polyethylene terephthalate synthetic polyesters
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Cutinase is used as a lipolytic enzyme in the composition of laundry and dishwashing detergents to more efficiently remove immobilized fats. The oleochemistry industries and pollutant degradation represent other potential uses of cutinase.
industry
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key for the design of biocatalysts with sufficient stability for practical applications in detergent industry
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions
industry
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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
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process
industry
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use of enzyme preadsorbed on cotton to esterify the hydroxyl groups of cellulose with the fatty acids from triolein. The cutinase-catalyzed esterification of the surface of cotton fabric leads to modified cotton fabric that shows a significant increase of hydrophobicity
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a high enzyme production, high specific enzyme activity, and high enzyme yield are obtained upon expression with a 5% air saturation of oxygen. At low dissolved oxygen concentration, enzyme yield and specific activity increase with increase of culture pH-value from 5.25 to 6.25
synthesis
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application of enginered mutant T101A/Q132A/I218A in synthetic fiber biotransformation
synthesis
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recombinant cutinase from Fusarium solani pisi is used as a catalyst in enzymatic transesterification between a mixture of triglyceride oils and methanol for biodiesel production in a bis(2-ethylhexyl) sodium sulfosuccinate (AOT)/isooctane reversed micellar system, kinetics, overview
synthesis
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immobilized cutinase HiC from the ascomycete Humicola insolens is applied as a biocatalyst for the synthesis of functionalized acryclic esters by transesterification using transesterification of methyl acrylate with 6-mercapto-1-hexanol at a high molar ratio in a solvent free system as a model reaction
synthesis
enzyme synthesizes butyl butanoate with a maximum esterification efficiency of 96.9% at 4 h
synthesis
expression of enzyme in Saccharomyces cerevisiae. Approximately 28% of the cutinase localizes to the cell walls and/or between cell wall and cell membrane. Protoplasts entrapped in a membrane capsule with a low-viscous liquid-core of 1.92 % w/v calcium-alginate in a static culture secrete measurable amounts of cutinase into the broth. The entrapped protoplasts are cultivated in a shake flask at low osmotic pressure without disruption. During 60 h of cultivation, the extracellular cutinase activity of the free protoplasts at 29.3 atm and protoplasts entrapped in the capsule at 17.2 atm are 0.13 and 0.39 U/mL, respectively
synthesis
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growth of Fusarium oxysporum MTCC 2480 on agro industrial wastes as inducer of cutinase production. Cutin isolated from peels of multi green colored watermelon yield 6.77 U/ml as compared to 9.64 U/ml of cutinase using apple cutin. The ester linkages in water melon cutin are completely hydrolyzed during submerged fermentation
synthesis
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synthesis of tyrosyl esters of various aliphatic fatty acids by a recombinant cutinase. The reaction system consists of an aqueous phase saturated with the corresponding fatty-acid vinyl ester. The maximum yield of tyrosyl butanoate achieved is 60.7% after 4 h at 20°C, pH 7.0
synthesis
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the cutinase exhibits strong synthetic activity for butyl butanoate in non-aqueous environment,under the optimized reaction conditions esterification efficiency of 95% is observed
synthesis
use of enzyme for polycondensation. Under thin film conditions the covalently immobilized enzyme catalyzes the synthesis of oligoesters of dimetil adipate with different polyols leading to Mw of about 1900 and Mn of about 1000. Immobilized Cut1 retains 37% of hydrolytic activity
synthesis
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use of enzyme for the synthesis of aliphatic esters. The maximum yield of ethyl caproate reaches 99.2% at a cutinase concentration of 50 U/ml, 40°C, and water content of 0.5%. The cutinase-catalyzed esterification displays strong tolerance for water content (up to 8%) and acid concentration (up to 0.8 M). Ester yields of more than 98% and 95% are achieved for acids of C3-C8 and alcohols of C1-C6, respectively
synthesis
Fusarium oxysporum MTCC 2480
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growth of Fusarium oxysporum MTCC 2480 on agro industrial wastes as inducer of cutinase production. Cutin isolated from peels of multi green colored watermelon yield 6.77 U/ml as compared to 9.64 U/ml of cutinase using apple cutin. The ester linkages in water melon cutin are completely hydrolyzed during submerged fermentation
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synthesis
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expression of enzyme in Saccharomyces cerevisiae. Approximately 28% of the cutinase localizes to the cell walls and/or between cell wall and cell membrane. Protoplasts entrapped in a membrane capsule with a low-viscous liquid-core of 1.92 % w/v calcium-alginate in a static culture secrete measurable amounts of cutinase into the broth. The entrapped protoplasts are cultivated in a shake flask at low osmotic pressure without disruption. During 60 h of cultivation, the extracellular cutinase activity of the free protoplasts at 29.3 atm and protoplasts entrapped in the capsule at 17.2 atm are 0.13 and 0.39 U/mL, respectively
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synthesis
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the cutinase exhibits strong synthetic activity for butyl butanoate in non-aqueous environment,under the optimized reaction conditions esterification efficiency of 95% is observed
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can be exploited in treating agricultural, food, and forest raw materials as well as their processing by-products
additional information
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can be exploited in treating agricultural, food, and forest raw materials as well as their processing by-products
additional information
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cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process
additional information
cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability
additional information
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cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability