Strategies and Recent Trends in Engineering Thermostable GH11 Xylanases
- Authors
- Kim, Beom Soo; Kim, In Jung
- Issue Date
- Mar-2025
- Publisher
- Multidisciplinary Digital Publishing Institute (MDPI)
- Keywords
- xylanase; glycoside hydrolase family 11; protein engineering; thermostability; artificial intelligence
- Citation
- Catalysts, v.15, no.4
- Indexed
- SCIE
SCOPUS
- Journal Title
- Catalysts
- Volume
- 15
- Number
- 4
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/78197
- DOI
- 10.3390/catal15040317
- ISSN
- 2073-4344
2073-4344
- Abstract
- Glycoside hydrolase family 11 (GH11) xylanases are used in various industries, such as biorefining, animal feed production, and baking, making them key industrial enzymes. Operating bioprocesses at elevated temperatures enhances the reaction rate and product yield and thus requires thermostable enzymes to sustain catalytic performance. The limited availability of naturally occurring thermostable GH11 xylanases necessitates targeted modifications via protein engineering to enhance their thermal stability. In this review, we present the key drivers of thermostability, an overview of engineering strategies, and the underlying mechanisms of action. Finally, we investigated state-of-the-art technologies involving artificial intelligence (AI)- and ancestral sequence reconstruction-guided approaches.
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