Work

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

Year: 2025

Type: article

Abstract: 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.

Source: iScience

DOI: 10.1016/j.isci.2025.114173