Engineering of Xylanases for the Development of Biotechnologically Important Characteristics
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Date
Authors
Şanlı Mohamed, Gülşah
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Open Access Color
Green Open Access
No
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Publicly Funded
No
Abstract
Xylanases are the main biocatalysts used for the reduction of the xylan backbone from hemicellulose, randomly splitting off β-1,4-glycosidic linkages between xylopyranosyl residues. Xylanase market has been annually estimated at 500 million US Dollars and they are potentially used in broad industrial process ranges such as paper pulp biobleaching, xylo-oligosaccharide production, and biofuel manufacture from lignocellulose. The highly stable xylanases are preferred in the downstream procedure of industrial processes because they can tolerate severe conditions. Almost all native xylanases can not endure adverse conditions thus they are industrially not proper to be utilized. Protein engineering is a powerful technology for developing xylanases, which can effectively work in adverse conditions and can meet requirements for industrial processes. This study considered state-of-the-art strategies of protein engineering for creating the xylanase gene diversity, high-throughput screening systems toward upgraded traits of the xylanases, and the prediction and comprehensive analysis of the target mutations in xylanases by in silico methods. Also, key molecular factors have been elucidated for industrial characteristics (alkaliphilic enhancement, thermal stability, and catalytic performance) of GH11 family xylanases. The present review explores industrial characteristics improved by directed evolution, rational design, and semi-rational design as protein engineering approaches for pulp bleaching process, xylooligosaccharides production, and biorefinery & bioenergy production.
Description
Keywords
Engineering xylanase, Biorefinery, Industrial characteristics, Pulp bleaching, XOs production, Endo-1,4-beta Xylanases, Protein Engineering
Fields of Science
0301 basic medicine, 0303 health sciences, 03 medical and health sciences
Citation
WoS Q
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OpenCitations Citation Count
14
Volume
120
Issue
Start Page
1171
End Page
1188
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Citations
CrossRef : 17
Scopus : 23
PubMed : 6
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Mendeley Readers : 22
SCOPUS™ Citations
23
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Web of Science™ Citations
21
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Page Views
577
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Downloads
36
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