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Updated: Jan 12, 2026

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
Published on: January 12, 2024
Backbone and Methyl resonance assignment of an active PETase
Jelena Grga1, Emmanuelle Boll2,3, Guy Lippens4
1Toulouse Biotechnology Institute (TBI), University of Toulouse, CNRS, INRAE, INSA Toulouse, 135 Avenue de Rangueil, 31077, Toulouse Cedex 04, France.
None:
LCCICCG, a bioengineered variant of a cutinase called LCC (Leaf-branch Compost Cutinase), is a high-performance, industrial-grade enzyme capable of efficiently degrading polyethylene terephthalate (PET). This engineered enzyme exhibits significantly enhanced thermal stability and PET hydrolysis activity compared to its predecessor and competing PETases. Here, we report the comprehensive resonance assignment of the polypeptide backbone and the side chain methyl groups of the active LCCICCG. Taking advantage of its exceptional thermostability all the experiments were conducted at 60 °C on a single, uniformly 15N-13C-labeled sample of this 27 kDa serine-hydrolase enzyme. LCCICCG represents a leap forward in enzymatic PET recycling, combining speed, efficiency, and scalability. The residue-specific information through both backbone and methyl side chain assignment represents a critical step toward detailed structural and dynamic NMR analyses.
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