期刊
CRITICAL REVIEWS IN BIOTECHNOLOGY
卷 30, 期 3, 页码 176-191出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/07388551003645599
关键词
Xylanase; heteroxylans; glycoside hydrolase family; substrate specificity; structure-function relationship; ligand binding; biotechnological applications
资金
- Instituut voor de aanmoediging van Innovatie door Wetenschap en Technologie in Vlaanderen (I.W.T., Brussels, Belgium)
- K.U. Leuven [GOA/03/10, IDO/03/005]
Xylanases are of widespread importance in several food and non-food biotechnological applications. They degrade heteroxylans, a structurally heterogeneous group of plant cell wall polysaccharides, and other important components in various industrial processes. Because of the highly complex structures of heteroxylans, efficient utilization of xylanases in these processes requires an in-depth knowledge of their substrate specificity. A significant number of studies on the three-dimensional structures of xylanases from different glycoside hydrolase (GH) families in complex with the substrate provided insight into the different mechanisms and strategies by which xylanases bind and hydrolyze structurally different heteroxylans and xylo-oligosaccharides (XOS). Combined with reports on the hydrolytic activities of xylanases on decorated XOS and heteroxylans, major advances have been made in our understanding of the link between the three-dimensional structures and the substrate specificities of these enzymes. In this review, authors gave a concise overview of the structure-function relationship of xylanases from GH5, 8, 10, and 11. The structural basis for inter- and intrafamily variation in xylanase substrate specificity was discussed as are the implications for heteroxylan degradation.
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