生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
総説
PET分解酵素Cut190の構造基盤と高機能化
織田 昌幸
著者情報
ジャーナル フリー

2020 年 60 巻 6 号 p. 342-345

詳細
抄録

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.

著者関連情報
© 2020 by THE BIOPHYSICAL SOCIETY OF JAPAN
前の記事 次の記事
feedback
Top