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Area of Science:

  • Biotechnology
  • Polymer Science
  • Enzymology

Background:

  • Enzymatic recycling of poly-l-lactic acid (PLLA) is gaining interest.
  • Limited understanding of enzymatic mechanisms and engineering strategies hinders PLLA depolymerization efficiency.

Purpose of the Study:

  • Identify and characterize subtilisins from Bacillus species for PLLA depolymerization.
  • Investigate mutations to enhance enzyme activity for improved PLLA biodegradation.
  • Understand the structural basis for enhanced enzymatic activity.

Main Methods:

  • Comparative mutational analysis of subtilisins from Bacillus pumilus and Bacillus subtilis.
  • In silico modeling to predict changes in enzyme structure and function.
  • Generation and testing of hyperactive enzyme variants for PLLA depolymerization.

Main Results:

  • A subtilisin from Bacillus pumilus was identified with high-molecular-weight PLLA depolymerization capability.
  • Mutational analysis revealed key residues enhancing enzyme activity.
  • Engineered variants showed significant increases in activity (830-fold for B. subtilis, 184-fold for B. pumilus).
  • In silico modeling indicated improved binding pocket accessibility and surface hydrophobicity.

Conclusions:

  • Subtilisins from Bacillus species are effective biocatalysts for PLLA depolymerization.
  • Enzyme engineering strategies can significantly enhance PLLA degradation.
  • Hyperactive variants demonstrate potential for practical applications in PLLA plastic recycling.