Trade-Offs between Stability and Activity of Glycosylated and Non-Glycosylated Polyester Hydrolases PHL7 and PHL7mut3.

ABSTRACT: Plastic pollution has become a global environmental challenge, driving interest in enzymatic polyethylene terephthalate (PET) recycling by using polyester hydrolases. In this study, we produced the PET-degrading enzyme PHL7 and its variant PHL7mut3 in Escherichia coli and Pichia pastoris (syn. Komagataella phaffii) to investigate the impact of N-glycosylation on enzyme properties. While glycosylation upon expression in P. pastoris enhanced thermal stability, it reduced the catalytic activity of the enzymes, revealing a trade-off that adds complexity to the selection of the best-suited expression system. Additionally, we engineered P. pastoris to produce non-glycosylated enzyme variants by substituting the asparagine residues (N) at all three putative N-gl

SUBMITTER: Fohler L 

PROVIDER: S-EPMC12624734 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature