Kyungpook National University Industry-Academic Cooperation Foundation

Industry-Academic Cooperation Foundation Gyeongsang National University

Kyung Jin Kim

Seon Won Kim

Zada Bakht

Seong Hee Jeong

A method for biologically producing acetin such as monoacetin, diacetin, or triacetin according to an embodiment of the present disclosure includes reacting acetyl-CoA with glycerol in the presence of a first O-acetyl transferase to obtain the acetin. With the method, acetin which is sustainable and safe, and has more excellent quality while not causing environmental pollution may be obtained.

Method for biologically producing acetin compound

Disclosed are a recombinant poly(ethylene terephthalate) hydrolase (PETase) expression vector, a recombinant mono(2-hydroxyethyl)terephthalate hydrolase (MHETase) expression vector, a strain for producing each of the recombinant PETase and MHETase containing each of the vectors, and a method for degrading a plastics using each of the recombinant PETase and MHETase expressed therefrom. When the recombinant hydrolases, that is, PETase and MHETase are used together, high enzymatic activity may be sustained for a long time to completely degrade the PET.

Recombinant PETase producing strain, recombinant MHETase producing strain, and composition for degrading PET containing the same

Disclosed are a method for preparing crystals of IsPETase protein, a method for screening an IsPETase protein activity regulator and IsPETase variants using a conformation of the protein crystal, a method for screening, IsPETase variants with increased PETase activity, and a method for decomposing PET using the variants. According to exemplary embodiments of the present invention, it is possible to determine a method for effectively preparing a crystal of the IsPETase protein and to obtain the resulting crystal thereof. Further, according to exemplary embodiments of the present invention, it is possible to identify a tertiary structure of the IsPETase from the crystal thereof and to prepare the variant with an increased PETase activity based on this structure. The IsPETase variant may be used effectively in the PET decomposition field.

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Daegu, South Korea

Kyung Jin Kim