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Insights into the mechanism of enzymatic hydrolysis of xylan.
- Source :
-
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2016 Jun; Vol. 100 (12), pp. 5205-14. Date of Electronic Publication: 2016 Apr 25. - Publication Year :
- 2016
-
Abstract
- Hemicelluloses are a vast group of complex, non-cellulosic heteropolysaccharides that are classified according to the principal monosaccharides present in its structure. Xylan is the most abundant hemicellulose found in lignocellulosic biomass. In the current trend of a more effective utilization of lignocellulosic biomass and developments of environmentally friendly industrial processes, increasing research activities have been directed to a practical application of the xylan component of plants and plant residues as biopolymer resources. A variety of enzymes, including main- and side-chain acting enzymes, are responsible for xylan breakdown. Xylanase is a main-chain enzyme that randomly cleaves the β-1,4 linkages between the xylopyranosyl residues in xylan backbone. This enzyme presents varying folds, mechanisms of action, substrate specificities, hydrolytic activities, and physicochemical characteristics. This review pays particular attention to different aspects of the mechanisms of action of xylan-degrading enzymes and their contribution to improve the production of bioproducts from plant biomass. Furthermore, the influence of phenolic compounds on xylanase activity is also discussed.
- Subjects :
- Biomass
Cellulose metabolism
Endo-1,4-beta Xylanases chemistry
Glycoside Hydrolases chemistry
Glycoside Hydrolases metabolism
Hydrolysis
Phenols
Plants chemistry
Polysaccharides metabolism
Substrate Specificity
Xylosidases chemistry
Endo-1,4-beta Xylanases metabolism
Xylans metabolism
Xylosidases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1432-0614
- Volume :
- 100
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Applied microbiology and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 27112349
- Full Text :
- https://doi.org/10.1007/s00253-016-7555-z