Enhanced Poly(ethylene terephthalate) Hydrolase Activity by Protein Engineering
نویسندگان
چکیده
منابع مشابه
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers.
Cutinase from Fusarium solani pisi was genetically modified near the active site, by site-directed mutagenesis, to enhance its activity towards polyethylene terephthalate (PET) and polyamide 6,6 (PA 6,6) fibers. The mutations L81A, N84A, L182A, V184A and L189A were done to enlarge the active site in order to better fit a larger polymer chain. Modeling studies have shown enhanced free energy sta...
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Protein adhesion and cell response to plasma-treated polymer surfaces were studied. The polymer polyethylene terephthalate (PET) was treated in either an oxygen plasma to make the surface hydrophilic, or a tetrafluoromethane CF(4) plasma to make the surface hydrophobic. The plasma source was radiofrequency (RF) discharge. The adsorption of albumin and other proteins from a cell-culture medium o...
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Cutinases have shown potential for hydrolysis of the recalcitrant synthetic polymer polyethylene terephthalate (PET). We have shown previously that the rate of this hydrolysis can be enhanced by the addition of hydrophobins, small fungal proteins that can alter the physicochemical properties of surfaces. Here we have investigated whether the PET-hydrolyzing activity of a bacterial cutinase from...
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1Austrian Centre of Industrial Biotechnology ACIB, 8010 Graz, Austria 8 2 Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, 9 Vienna, 3430 Tulln, Austria 10 3 Microbiology Group, Research Area Biotechnology and Microbiology, Institute of Chemical 11 Engineering, Vienna University of Technology, 1060 Vienna, Austria. 12 4 Institute of Biotechnology, Uni...
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Dynamic mechanical thermal analysis performed on cold-drawn polyethylene terephthalate PET , cold crystallized annealed in the temperature interval 100–140 °C, reveals the presence of marginally glassy domains above the annealing temperature Ta. This suggests that the thermodynamic force driving crystallization causes the structural arrest of some noncrystalline domains. The latter thus need a ...
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ژورنال
عنوان ژورنال: Engineering
سال: 2018
ISSN: 2095-8099
DOI: 10.1016/j.eng.2018.09.007