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
-
lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
-
polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
-
monilinia
-
terephthalic
- petase
- synthesis
- nectria
-
hydrophobins
-
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
ECTree
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Purification
Purification on EC 3.1.1.74 - cutinase
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by immobilized metal affinity chromatography exploiting a C-terminal His-tag
native extracellular enzyme 1.42fold to homogeneity by ammoium sulfate fractionation, cation exchange chromatography, and two steps of gel filtration
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optimization and evaluation of foam fractionation as purification method to purify an extracellular cutinase from untreated supernatant of mycelium of submerged cultures of the basidiomycete Coprinopsis cinerea as a model enzyme, detailed overview
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osmotic shock, acid precipitation, dialysis and two sequential anion exchange chromatographic steps, followed by a final dialysis and subsequently freeze-dried. Cutinase purity is confirmed by 12.5% SDS-PAGE
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purification includes cationic Expanded Bed Adsorption (EBA) followed by hydrophobic interaction chromatography (HIC)
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recombinant C-terminally His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
recombinant C-terminally His-tagged wild-type and mutant cutinases lacking the signal peptide sequence 1.9fold from Escherichia coli strain BL21(DE3) culture supernatant by ammonium sulfate fractionation and nickel affinity chromatography
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recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) culture supernatant by nickel affinity chromatography to homogeneity
recombinant cutinase isozymes Tfu 0882 and Tfu 0883 from Escherichia coli strain BL21(DE3)
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recombinant enzyme from Escherichia coli strain BL21-Gold(DE3)
recombinant enzyme from Pichia pastoris strain X-33culture supernatant by tangential flow filtration and filter cell-based ultrafiltration
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recombinant enzyme partially 293fold from Pichia pastoris strain X-33 by ultrafiltration
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recombinant extracellular enzyme 2.0fold from culture supernatant by ammonium sulfate precipitation and two different steps of anion exchange chromatography
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recombinant extracellular wild-type and mutant enzymes without a putative N-terminal signal peptide (Met1-Ala34) and Gln35 from Escherichia coli
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity and anion exchange chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Origami B (DE3) by nickel affinity chromatography, tag cleavage by recombinant enterokinase, and anion exchange chromatography
study of enzyme partition in a 20% polyethylene glykol/15% phosphate two-phase system. Specific interaction of butyrate to the active site of enzyme, enzyme-butyrate complex is over two times the size of the free enzyme
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wild-type and mutants purified by ultrafiltration, wild-type further purified by hydrophobic interaction chromatography and ammonium sulfate precipitation, 1.6fold with a yield of 70%