Team:TJUSLS China/proposed
Proposed implementatior
Proposed implementation
Basing on the structural information of IsPETase and the theory of rational design, we developed a series of protein engineering strategy using several IsPETase variants that were screened for high thermal stability to improve PET degradation activity. The designed structural modifications will then be further verified through a proper evaluation strategy.
Proof of concept
PET is used extensively worldwide. However, the ability to enzymatically degrade PET, especially highly crystallized PET, has been thought to be limited to a few hydrolase. Although IsPETase has the highest degradation activity of highly crystallized PET under mild conditions of all PET-degrading enzymes reported to date, its low thermal stability limits its ability for efficient and practical enzymatic degradation of PET. Considering the glass transition temperature of PET is around 75°C, above which the polyester chain of PET performs in a high elastic state where the degradation is promoted, thus, higher thermal stability will enable IsPETase to degrade highly crystallized PET more efficiently.