Thermostability Enhancement of GH 62 α‑l‑Arabinofuranosidase by Directed Evolution and Rational Design

Thermostability Enhancement of GH 62 α‑l‑Arabinofuranosidase by Directed Evolution and Rational Design

GH 62 arabinofuranosidases are known for their excellent specificity for arabinoxylan of agroindustrial residues and their synergism with endoxylanases and other hemicellulases. However, the low thermostability of some GH enzymes hampers potential industrial applications. Protein engineering researc...

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Veröffentlicht in:Journal of agricultural and food chemistry 2024-02, Vol.72 (8), p.4225-4236
Hauptverfasser: Martins, Manoela, dos Santos, Alberto M., da Costa, Clauber H. S., Canner, Samuel W., Chungyoun, Michael, Gray, Jeffrey J., Skaf, Munir S., Ostermeier, Marc, Goldbeck, Rosana
Format: Artikel
Sprache:eng
Schlagworte:
Biotechnology and Biological Transformations
Enzyme Stability
Glycoside Hydrolases
Mutagenesis
Protein Engineering
Temperature
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Zusammenfassung:GH 62 arabinofuranosidases are known for their excellent specificity for arabinoxylan of agroindustrial residues and their synergism with endoxylanases and other hemicellulases. However, the low thermostability of some GH enzymes hampers potential industrial applications. Protein engineering research highly desires mutations that can enhance thermostability. Therefore, we employed directed evolution using one round of error-prone PCR and site-saturation mutagenesis for thermostability enhancement of GH 62 arabinofuranosidase from Aspergillus fumigatus. Single mutants with enhanced thermostability showed significant ΔΔG changes (
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.3c08019