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Abstract

The extracellular cellulases from the anaerobic bacterium Clostridium thermocellum and the anaerobic rumen fungus Neocallimastix frontalis are very active on crystalline cellulose. In both cases the activity resides in a high molecular weight complex. The complex from C.thermocellum (termed the cellulosome), which despite extensive study throughout the world has hitherto been impossible to dissociate without loss of nearly all activity to crystalline cellulose, was found, after careful observation and measurement in the present study, to be readily dissociated at pH 5.0 and at room temperature by a mixture of SDS, EDTA and DTT. Furthermore, virtually all the activity of the unfractionated cellulosome was recovered when the dissociated enzyme components were reassociated by dialysis against Tris buffer, pH 7.0 containing DTT. Thus, the route is now established for the first time for a meaningful study of the mechanism of cellulase action of this commercially important enzyme system. The specific activity of the partially purified enzyme for degradation of crystalline cellulose was several-fold greater than that produced by the aerobic fungus T. reesei, which is being developed world-wide for its commercial potential for converting cellulose to fermentable soluble sugars.

Additional information

Authors: BHAT K M, Rowett Research Institute, Aberdeen (GB);GOW L A, Rowett Research Institute, Aberdeen (GB);WILSON C A, Rowett Research Institute, Aberdeen (GB);WOOD T W, Rowett Research Institute, Aberdeen (GB)
Bibliographic Reference: EUR 12717 EN (1990) 121 pp., MF, ECU 8, blow-up copy ECU 16.25
Availability: (2)
Record Number: 199011135 / Last updated on: 1994-12-01
Category: PUBLICATION
Original language: en
Available languages: en