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Characterization of C-terminally engineered laccases.

Yingli Liu1, Angela Maria Cusano2, Erin C Wallace3

  • 1Beijing Laboratory for Food Quality and Safety, Beijing Technology & Business University (BTBU), Beijing 100048, China; Aix Marseille Université, CNRS, iSm2 UMR 7313, 13397 Marseille, France.

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Modifying the carboxy terminus of Trametes sp. LAC3 laccase affects its catalytic efficiency. However, glycosylation and terminal functionalization of this laccase are viable strategies for enzyme applications.

Keywords:
GlycosylationMulti-copper enzymeTagged protein

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Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Engineering

Background:

  • Protein termini are crucial for functionalization and modification.
  • Laccases are versatile enzymes with broad industrial applications.
  • Understanding enzyme terminal modifications is key to optimizing their performance.

Purpose of the Study:

  • To investigate the impact of carboxy terminus modifications on LAC3 laccase activity.
  • To explore the role of glycosylation in enzyme function and stability.
  • To assess the suitability of laccase termini for functionalization and immobilization.

Main Methods:

  • Generation and production of carboxy terminus variants (CΔ, CΔ6H) in Saccharomyces cerevisiae.
  • Purification and characterization of wild-type and modified laccase forms (CΔ6Hh).
  • Enzymatic activity assays using syringaldazine and ABTS substrates to determine kinetic parameters (kcat, KM).

Main Results:

  • Carboxy terminus deletion (CΔ) moderately decreased catalytic efficiency (4-10 fold).
  • 6 His-tagged (CΔ6H) and hyper-glycosylated (CΔ6Hh) variants showed comparable catalytic efficiency to wild-type.
  • In vitro deglycosylation significantly reduced laccase activity, highlighting the importance of glycosylation.

Conclusions:

  • Laccase terminal sequences are suitable for functionalization and immobilization.
  • Over-glycosylation does not negatively impact catalytic efficiency.
  • Glycosylation plays a vital role in maintaining laccase activity.