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<p>LCC<sup>ICCG</sup>, 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 LCC<sup>ICCG</sup>. Taking advantage of its exceptional thermostability all the experiments were conducted at 60&#xa0;°C on a single, uniformly <sup>15</sup>N-<sup>13</sup>C-labeled sample of this 27&#xa0;kDa serine-hydrolase enzyme. LCC<sup>ICCG</sup> 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.</p>

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Backbone and Methyl resonance assignment of an active PETase

  • 期刊论文

  • 发表日期：

    2025年11月5日

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  • Jelena Grga,
  • Emmanuelle Boll,
  • Guy Lippens,
  • Cyril Charlier

摘要

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.