Degradation and ring-opening polymerization of poly(ε-caprolactone) by a novel enzyme from Pseudomonas sp. DS0801.

Poly(ε-caprolactone) (PCL) is a widely used synthetic polymer with significant commercial applications, and its degradation and synthesis have become the focus of considerable research. In this study, we purified a PCL-degrading enzyme, PCLase0801, produced by Pseudomonas sp. DS0801. The enzyme was purified to homogeneity and had a molecular weight of 30.4 kDa. It exhibited optimal activity at 40°C and pH 8.0, hydrolyzing PCL into monomers, dimers, and trimers. The enzyme was identified as a lipase and showed good tolerance to organic solvents. Additionally, PCLase0801 catalyzed the ring-opening polymerization of ε-caprolactone, producing PCL with a molecular weight of 6050 g/mol and favorable structural properties. This work provides new insights into the potential applications of PCL-degrading enzymes in PCL treatment and biosynthesis.