21
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Purification and partial characterization of two extracellular endoglucanases from Cellulomonas fermentans.

      , ,
      Biochemical and biophysical research communications
      Elsevier BV

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Avicelase assay of gel slices after non-denaturing polyacrylamide gel electrophoresis of concentrated supernatants from Cellulomonas fermentans revealed four active bands. One of them corresponded to the principal active band on CM-cellulose. Among the three others, at least one did not correspond to any active band on CM-cellulose and might reflect the presence of an exoglucanase (EC 3.2.1.91). The active band on CM-cellulose was composed of two endoglucanases (EC 3.2.1.4), called CFA and CFB, which we purified by the means of DEAE-Trisacryl chromatography and high performance liquid chromatography (anion exchange chromatography and gel chromatography). These two monomeric enzymes differ in their molecular weights (40,000 and 57,000 for CFA and CFB, respectively) and in their catalytic constants in the reaction with CM-cellulose (Km were 1.5 g/l and 59 g/l for CFA and CFB, respectively), but have similar modes of action on this substrate and similar substrate specificities.

          Related collections

          Author and article information

          Journal
          Biochem Biophys Res Commun
          Biochemical and biophysical research communications
          Elsevier BV
          0006-291X
          0006-291X
          Oct 15 1986
          : 140
          : 1
          Article
          0006-291X(86)91079-X
          10.1016/0006-291x(86)91079-x
          3096318
          f298026a-6bc1-49b2-a750-2f8c64281cc5
          History

          Comments

          Comment on this article