Insights into the mechanism of enzymatic hydrolysis of xylan
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...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2016-06, Vol.100 (12), p.5205-5214 |
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| description | 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. |
| doi_str_mv | 10.1007/s00253-016-7555-z |
| format | Article |
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R. S. ; Filho, E. X. F.</creator><creatorcontrib>Moreira, L. R. S. ; Filho, E. X. F.</creatorcontrib><description>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. 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R. S.</creatorcontrib><creatorcontrib>Filho, E. X. F.</creatorcontrib><title>Insights into the mechanism of enzymatic hydrolysis of xylan</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>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.</description><subject>Acids</subject><subject>Biochemistry</subject><subject>Biomass</subject><subject>Biomedical and Life Sciences</subject><subject>Biopolymers</subject><subject>Biotechnology</subject><subject>Cellulose</subject><subject>Cellulose - metabolism</subject><subject>Chemical bonds</subject><subject>Chemical properties</subject><subject>Chemical research</subject><subject>Endo-1,4-beta Xylanases - chemistry</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzymes</subject><subject>Fungi</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Hydrolysis</subject><subject>Life Sciences</subject><subject>Lignin</subject><subject>Lignocellulose</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mini-Review</subject><subject>Phenols</subject><subject>Plant biomass</subject><subject>Plants - chemistry</subject><subject>Polysaccharides - metabolism</subject><subject>Studies</subject><subject>Substrate Specificity</subject><subject>Xylans</subject><subject>Xylans - metabolism</subject><subject>Xylosidases - chemistry</subject><subject>Xylosidases - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkl1rFDEUhoModlv9Ad7IgDf2YmqSmSQT8KYUPxYKgh_XIZM52U2ZSWqSgc7-erNuLa4okovAOc_7ck7yIvSC4AuCsXiTMKasqTHhtWCM1btHaEXahtaYk_YxWmEiWOnI7gSdpnSDMaEd50_RCRWE0KaVK_R27ZPbbHOqnM-hyluoJjBb7V2aqmAr8Ltl0tmZarsMMYxLcmlfv1tG7Z-hJ1aPCZ7f32fo2_t3X68-1tefPqyvLq9rw9om13bQEjreg5S2hd5SCdD3mAvWyIGY1jQDl9qAMcYORljCCNVW4B6MFJ2mzRl6ffC9jeH7DCmrySUDYxkBwpwU6XDHKaZY_B8VEsvyaFwW9NUf6E2Yoy-L_KRoQ5oy_gO10SMo523IUZu9qbpsGS1eHSeFuvgLVc4AkzPBg3WlfiQ4PxIUJsNd3ug5JbX-8vmYJQfWxJBSBKtuo5t0XBTBah8EdQiCKkFQ-yCoXdG8vF9u7icYHhS_fr4A9ACk0vIbiL9t_0_XH-KYu_M</recordid><startdate>20160601</startdate><enddate>20160601</enddate><creator>Moreira, L. 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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. 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| subjects | Acids Biochemistry Biomass Biomedical and Life Sciences Biopolymers Biotechnology Cellulose Cellulose - metabolism Chemical bonds Chemical properties Chemical research Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - metabolism Enzymes Fungi Glycoside Hydrolases - chemistry Glycoside Hydrolases - metabolism Hydrolysis Life Sciences Lignin Lignocellulose Microbial Genetics and Genomics Microbiology Mini-Review Phenols Plant biomass Plants - chemistry Polysaccharides - metabolism Studies Substrate Specificity Xylans Xylans - metabolism Xylosidases - chemistry Xylosidases - metabolism |
| title | Insights into the mechanism of enzymatic hydrolysis of xylan |
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