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      Xylanases, xylanase families and extremophilic xylanases.

      1 , ,
      FEMS microbiology reviews
      Elsevier BV

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          Abstract

          Xylanases are hydrolytic enzymes which randomly cleave the beta 1,4 backbone of the complex plant cell wall polysaccharide xylan. Diverse forms of these enzymes exist, displaying varying folds, mechanisms of action, substrate specificities, hydrolytic activities (yields, rates and products) and physicochemical characteristics. Research has mainly focused on only two of the xylanase containing glycoside hydrolase families, namely families 10 and 11, yet enzymes with xylanase activity belonging to families 5, 7, 8 and 43 have also been identified and studied, albeit to a lesser extent. Driven by industrial demands for enzymes that can operate under process conditions, a number of extremophilic xylanases have been isolated, in particular those from thermophiles, alkaliphiles and acidiphiles, while little attention has been paid to cold-adapted xylanases. Here, the diverse physicochemical and functional characteristics, as well as the folds and mechanisms of action of all six xylanase containing families will be discussed. The adaptation strategies of the extremophilic xylanases isolated to date and the potential industrial applications of these enzymes will also be presented.

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          Author and article information

          Journal
          FEMS Microbiol Rev
          FEMS microbiology reviews
          Elsevier BV
          0168-6445
          0168-6445
          Jan 2005
          : 29
          : 1
          Affiliations
          [1 ] Laboratory of Biochemistry, Institute of Chemistry B6, University of Liège, B-4000 Liège, Belgium. tcollins@ulg.ac.be
          Article
          S0168-6445(04)00050-6
          10.1016/j.femsre.2004.06.005
          15652973
          cb38b7cd-aba3-46e5-b915-c753ab2bde1f
          History

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