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| Main Authors: | , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Journal of agricultural and food chemistry
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40977531/ |
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Table of Contents:
- Binding Stability and Catalytic Mechanism of a Novel Chitin Deacetylase from and Preparation of Chitosan. Liang, Bicheng Zhang, Tong Li, Guantian Yang, Haoyue Wang, Zongji Li, Kecheng Liu, Song Yu, Huahua Xing, Ronge Chitosan Amidohydrolases Bacterial Proteins Enzyme Stability Molecular Docking Simulation Biocatalysis Molecular Dynamics Simulation Chitin Kinetics Hydrogen-Ion Concentration Protein Binding This study reports the heterologous expression, purification, and functional characterization of a novel chitin deacetylase (CDA) from . The recombinant CDA exhibited optimal activity at pH 7 and 35 °C, with Mg enhancing its function. Deep eutectic solvent (DES) pretreatment significantly improved chitin accessibility, enabling CDA to produce chitosan with a high degree of deacetylation (71.2%) and recovery rate (14.2%). Structural analyses confirmed reduced crystallinity and successful acetyl removal. Molecular docking and dynamics simulations identified Asp318, His470, and Trp433 as key catalytic residues with stable binding to (GlcNAc). These findings highlight CDA's potential for eco-friendly chitosan production and provide a basis for future enzyme engineering.