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Insights into the mechanism of enzymatic hydrolysis of xylan

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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.

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Acknowledgments

The author acknowledges the receipt of financial support from the Brazilian National Council for Scientific and Technological Development (CNPq), Coordination for the Improvement of Higher Education Personnel (CAPES) Foundation for Research Support of the Federal District (FAPDF), and the National Institute for Science and Technology of Bioethanol.

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  1. Laboratory of Enzymology, Cellular Biology Department, University of Brasília, CEP, Brasília, DF, 70910-900, Brazil

    L. R. S. Moreira & E. X. F. Filho

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  1. L. R. S. Moreira
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Correspondence to L. R. S. Moreira.

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Dra. Leonora Moreira and Dr. Edivaldo Ferreira Filho declare no conflict of interest.

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Moreira, L.R.S., Filho, E.X.F. Insights into the mechanism of enzymatic hydrolysis of xylan. Appl Microbiol Biotechnol 100, 5205–5214 (2016). https://doi.org/10.1007/s00253-016-7555-z

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