著者

織田 昌幸

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.60, no.6, pp.342-345, 2020 (Released:2020-11-28)

参考文献数

14

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A cutinase-like enzyme from a thermophilic isolate, Saccharomonospora viridis AHK190, Cut190, has the ability to depolymerize polyethylene terephthalate (PET). The catalytic activity and thermal stability of Cut190 are increased by Ca2+ binding. The structural analysis of Cut190 mutants in complex with metal ions and substrates elucidated the reaction mechanism regulated by Ca2+. The metal ion-binding properties, analyzed using isothermal titration calorimetry were correlated with the effects on Cut190 activity and stability, which could be improved using protein engineering. The Cut190 mutant will be used for PET chemical recycling.