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Insights into the mechanism of enzymatic hydrolysis of xylan.

Authors :
Moreira LR
Filho EX
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.

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