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March 22, 2026CatalystsOpen Access

Improving Process Stability and Activity of B. subtilis GH46 Chitosanase via Directed Evolution: Insights into Active-Site Cleft Dynamics

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Authors

RMRonny MartínezCVClaudia VásquezVVValeria Vásquez

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Overview

Directed evolution improves chitosanase activity in Bacillus subtilis, suggesting pathways for industrial application.

Key Points

  • The goal is to enhance the functionality of chitosanases for better performance in industrial applications.
  • Conducted directed evolution on Bacillus subtilis chitosanase across three rounds of screening.
  • Screened approximately 9000 clones to identify variants with improved activity.
  • Analyzed enzyme performance using HPLC, DLS, and MALDI-TOF.
  • Performed molecular dynamics simulations and docking studies to investigate active-site cleft dynamics.
  • Identified three variants (MT1, MT2, MT3) with increased specific activity and thermal stability.
  • Observed significant improvements in Vmax and T1/2 at 60 °C for selected variants.
  • HPLC and DLS analyses showed narrower size distribution and lower average molecular weight of COS products.

Cite This Study

Martínez et al. (2026) studied this question.

synapsesocial.com/papers/69bf899af665edcd009e9604https://doi.org/10.3390/catal16030280
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