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Illustration of PET hydrolase (PETase, left) and MHET hydrolase (MHETase, right), two plastic-degrading enzymes from the bacterium Ideonella sakaiensis. I. sakaiensis was discovered in 2016 in sediment near a plastic bottle recycling facility in Japan. It is able to use the plastic polyethylene terephthalate (PET) as its primary energy source. PETase converts PET (top left) to the smaller molecule mono(2-hydroxyethyl) terephthalic acid (MHET, top centre). MHET is then further broken down by MHETase to terephthalic acid (TPA, top right) and ethylene glycol (below TPA). The products of this degradation are environmentally harmless. For an unlabelled version of this image see F037/3626.
2023-02-04
JUAN GAERTNER/Science Photo Library RF/East News
Science Photo Library RF
JUAN GAERTNER
f0373625
5,69MB
68cm x 51cm przy 300dpi
2-HYDROXYETHYL, 3D, ACID, ACTIVE, ARTWORK, BACKGROUND, BACTERIAL, BIOACCUMULATION, BIOCHEMICAL, BIOCHEMISTRY, BIODEGRADATION, BIOLOGICAL, BIOLOGY, BIOREMEDIATION, BIOTECHNOLOGY, BLUE, CATALYSIS, CATALYTIC, CGI, CONTAMINATION, DEGRADATION, DEGRADER, DEGRADERS, DEPOLYMERIZATION, DIGITALLY, EATING, ENGINEERING, ENVIRONMENT, ENVIRONMENTAL, ENZYMATIC, ENZYME, ETHYLENE, GAERTNER, GENERATED, GENETIC, GLYCOL, HYDROLASE, ILLUSTRATION, JUAN, LABEL, LABELED, LABELLED, LABELS, MHET, MHETASE, MICROBIAL, MICROBIOLOGICAL, MICROBIOLOGY, MODEL, MOLECULAR, MOLECULE, MONO, monohydroxyethyl, NO-ONE, NOBODY, PAIR, PET, PETASE, PLASTIC, PLASTIC-EATING, POLLUTION, POLY, POLYETHYLENE, POLYMER, POLYMERISATION, PROTEIN, RECYCLING, SITE, SOLUTION, STRUCTURE, TEREPHTHALATE, TEREPHTHALIC, TEXT,