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a-Synuclein: A fusion chaperone significantly boosting the enzymaticperformance of pet hydrolase

Chinese Journal of Chemical Engineering 2023年第12期64卷 18-25页

作者： Renwen Tian Yan Sun Department of Biochemical Engineering School of Chemical Engineering and Technology and Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology(Ministry of Education)Tianjin UniversityTianjin 300350China

Extensive use of polyethylene terephthalate (pet) has brought about global environmental problems. Arecently reported pet hydrolase (petase) discovered from Ideonella sakaiensis showed high potentialfor degrading pet at moderate temperatures, but its activity and stability need further improvementfor practical applications. Herein, we proposed to use a-synuclein (aS) as a fusion chaperone and createdsix petase-aS fusion enzymes with linkers of different types and lengths. All the fusion enzymes exhibited improved enzymatic performance, presenting 1.5 to 2.6-fold higher activity towards bis-2(hydroxyethyl) terephthalate than petase, as well as significantly increased stabilities. Fluorescencespectroscopy indicated that the chaperone fusion tightened the overall conformation and resulted inthe opening of the substrate binding pocket, which led to the improved thermal stability and catalyticactivity of the fusion enzymes. Remarkably, one of the fusion proteins, petase-[(GS)(EK)]10-aS, showed3.2 to 5.1 times higher pet degradation capability than petase. The significantly boosted pet degradationperformance was not only attributed to the enhanced enzymatic activity and stability, but also possiblydue to the binding affinity of the fused aS domain for pet. These findings demonstrated that aS was aneffective fusion chaperone for significantly enhancing the enzymatic performance of petase.

关键词： pet hydrolase a-Synuclein Fusion enzyme Stability Pollution Degradation

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