Structural and functional characterization of an auxiliary domain-containing PET hydrolase from Burkholderiales bacterium

• Published in: Journal of hazardous materials Vol. 429; p. 128267
• Main Authors: Sagong, Hye-Young, Kim, Seongmin, Lee, Donghoon, Hong, Hwaseok, Lee, Seul Hoo, Seo, Hogyun, Kim, Kyung-Jin
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 05.05.2022
• Subjects: Auxiliary domain; Biological degradation; Burkholderiales - metabolism; Hydrolases - metabolism; Hydrolysis; PET hydrolase; Polyethylene terephthalate; Polyethylene Terephthalates - chemistry; Polyethylene Terephthalates - metabolism; Polyethylene terephthalate; PET hydrolase; Biological degradation; Auxiliary domain
• ISSN: 0304-3894; 1873-3336
• DOI: 10.1016/j.jhazmat.2022.128267

Biodegradation of polyethylene terephthalate (PET) is one of fundamental ways to solve plastic pollution. As various microbial hydrolases have an extra domain unlike PETase from Ideonella sakaiensis (IsPETase), research on the role of these extra domain in PET hydrolysis is crucial for the identification and selection of a novel PET hydrolase. Here, we report that a PET hydrolase from Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36 (BbPETase) with an additional N-terminal domain (BbPETaseAND) shows a similar hydrolysis activity toward microcrystalline PET and a higher thermal stability than IsPETase. Based on detailed structural comparisons between BbPETase and IsPETase, we generated the BbPETaseS335N/T338I/M363I/N365G variant with an enhanced PET-degrading activity and thermal stability. We further revealed that BbPETaseAND contributes to the thermal stability of the enzyme through close contact with the core domain, but the domain might hinder the adhesion of enzyme to PET substrate. We suggest that BbPETase is an enzyme in the evolution of efficient PET degradation and molecular insight into a novel PET hydrolase provides a novel strategy for the development of biodegradation of PET. [Display omitted] •Investigation of an auxiliary domain-containing PET hydrolase.•Development of a PET hydrolase with enhanced enzyme activity and thermal stability.•Structural and functional roles of auxiliary domain in PET decomposition.