Analytical Data
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Gene name
PET hydrolase
- Application
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Alternative Names
Cutinase cut1; Poly(ethylene terephthalate) hydrolase; PET hydrolase; PETase; 3.1.1.101; cut_1; Thermobifida fusca; Thermomonospora fusca; Hydrolase; Serine esterase; 3.1.1.74
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Species
Others
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
G8GER6
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Expression Region
A59-F319
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Protein Length
Full Length of Mature Protein
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Polyethylene terephthalate (PET) is a widely used synthetic polymer that poses significant environmental challenges due to its durability and resistance to degradation. The accumulation of PET waste has prompted extensive research into effective biodegradation methods, particularly through the use of enzymes that can break down polyester materials. Among these enzymes, PET hydrolases have garnered considerable attention for their ability to catalyze the hydrolysis of PET into its constituent monomers, such as terephthalic acid and ethylene glycol. The identification and characterization of PET hydrolases from various microorganisms, such as the bacterium *Ideonella sakaiensis*, represent a promising avenue for developing biotechnological solutions to plastic waste management. Recent advances in recombinant protein technology have enabled the production of engineered PET hydrolases with enhanced activity and stability, paving the way for their application in industrial settings. Research in this field aims to optimize these enzymes for more efficient PET recycling processes, contributing to a circular economy and reducing the ecological footprint of plastic materials. Additionally, understanding the mechanisms of PET degradation at the molecular level could lead to the discovery of novel enzymes with improved properties, further enhancing the bioremediation potential of these biological catalysts.
