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Preparative purification of Trichoderma reesei native and {open_quotes}core{close_quotes} cellobiohydrolase I by electrophoresis and chromatofocusing

Conference ·
OSTI ID:431596
; ;  [1]
  1. Oak Ridge National Lab., TN (United States)
The enzymes present in the cellulose complex produced by the fungus Trichoderma reesei have been the subject of considerable attention in consequence of their potential for converting cellulosic materials into glucose for further use in fermentation processes. Cellobiohydrolase I (CBH I) is the major component of crude commercial fungal cellulose preparations and catalyzes the conversion of insoluble cellulose into cellobiose. The primary structure of CBH I is known, and its tertiary structure, deduced from small-angle X-ray scattering studies, takes the shape of a tadpole with a catalytic head region known as {open_quotes}core{close_quotes} CBH I and a C-terminal cellulose-binding tail region. Removal of the tail can be accomplished with the protease papain, resulting in reduced activity towards insoluble substrates but unchanged activity towards soluble substrates.
Research Organization:
Oak Ridge National Lab., TN (United States); Badger Engineers, Inc., Tampa, FL (United States); Solar Energy Research Inst., Golden, CO (United States)
OSTI ID:
431596
Report Number(s):
CONF-900512--
Country of Publication:
United States
Language:
English