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  1. 23 de may. de 2024 · The enzyme Goddard’s lab is working with evolved within the bacteria Ideonella sakaiensis, which breaks down PET plastics in nature. It was discovered by a team of Japanese scientists outside a landfill and reported in Science in 2016.

  2. 10 de may. de 2024 · Here, we investigate the effects of surface charge point mutations both proximal and distal to the active site of the mesophilic PET-degrading enzyme from Ideonella sakaienses (IsPETase) and an engineered thermostable variant with superior activity, STAR PETase.

  3. 14 de may. de 2024 · The recent discovery of a soil bacterium, Ideonella sakaiensis, capable of secreting PET depolymerizing enzymes (Fig. 1a, b) that can cleave the ester bonds of PET, has truly revolutionized the field, opening up new possibilities for the development of economically viable bio-based recycling processes for PET (Yoshida et al. 2016).

  4. Hace 2 días · The second, Ideonella sakaiensis, produces enzymes that enable it to break down and metabolize PET. The upcycling would be accomplished via a second step – using the second E. coli strain engineered with CRISPR-Cas9 gene-editing technology to create products such as adipic acid, a material found in many useful products, including nylon, drugs and even fragrances.

  5. 7 de may. de 2024 · El interés en la PETasa surgió en 2016, cuando un grupo de científicos japoneses, bajo el liderazgo de Shosuke Yoshida, identificó una nueva especie de bacteria llamada “Ideonella sakaiensis”, capaz de usar el tereftalato de polietileno como fuente de carbono y energía: en otras palabras, capaz de alimentarse de PET.

  6. 9 de may. de 2024 · In a previous study regarding Ideonella sakaiensis 201-F6 (Yoshida et al., 2016), three products were generated, including terephthalic acid (TPA), mono-(2-hydroxyethyl) terephthalate (MHET), and bis (2-hydroxyethyl) terephthalate (BHET), among which MHET was the primary PET hydrolysis product (Yoshida et al., 2016).

  7. 10 de may. de 2024 · Here, we investigate the effects of surface charge point mutations both proximal and distal to the active site of the mesophilic PET-degrading enzyme from Ideonella sakaienses (IsPETase) and an engineered thermostable variant with superior activity, STAR PETase.