Purification and Characterization of an Endoglucanase from the Cellulosomes (Multicomponent Cellulase Complexes) of Clostridium thermocellum

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概要

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• A subunit with carboxymethyl cellulase (CMCase) activity was isolated from the cellulosomes of Clostridium thermocellum after dissociation of the cellulosomes by a mild sodium dodecyl sulfate (SDS) treatment. The subunit displayed only one protein band of 51kDa on SDS-polyacrylamide gel electrophoresis (SDS-PAGE), but after boiling with SDS it had 3 bands of 60,56,and 48 kDa. Prolonged incubation with SDS changed the subunit to display exclusively the 48-kDa band after boiling. The 51-kDa subunit was presumably a partially denatured form, and differentiated into 3 species with apparent M_r of 60,56,and 48k through deglycosylation in SDS solution. Enzymatic properties of the 51-kDa subunit resembled those of the endoglucanase A which was purified from the culture fluid and from a E. coli clone with exceptions of temperature and pH optima.

• 1992-08-23

著者

• Mori Yutaka

  Chugoku National Agricultural Experiment Station

関連論文

• Accumulation of γ-Aminobutyric Acid (Gaba) in the Rice Germ during Water Soaking
• Purification and Characterization of an Endoglucanase from the Cellulosomes (Multicomponent Cellulase Complexes) of Clostridium thermocellum

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