Enzymatic surface hydrolysis of PET : effect of structural diversity on kinetic properties of cutinases from thermobifida
作者： Enrique Herrero Acero , Doris Ribitsch , Georg Steinkellner , Karl Gruber , Katrin Greimel
DOI: 10.1021/MA200949P
关键词:
摘要: In this study cutinases from Thermobifida cellulosilytica DSM44535 (Thc_Cut1 and Thc_Cut2) fusca DSM44342 (Thf42_Cut1) hydrolyzing poly(ethylene terephthalate) (PET) were successfully cloned expressed in E.coli BL21-Gold(DE3). Their ability to hydrolyze PET was compared with other enzymes natural polyesters, including the PHA depolymerase (ePhaZmcl) Pseudomonas fluorescens two T. KW3. The three isolated are very similar (only a maximum of 18 amino acid differences) but yet had different kinetic parameters on soluble substrates. kcat Km values pNP–acetate ranges 2.4–211.9 s–1 127–200 μM while pNP–butyrate they showed between 5.3 195.1 1483 2133 μM. Thc_Cut1 released highest amounts MHET terephthalic bis(benzoyloxyethyl) terephthalate (3PET) concomitant increase hydrophilicity as indicated by water co...
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