Characterization of the Subunits in an Apparently Homogeneous Subpopulation of Clostridium-Thermocellum Cellulosames

Ali, Bassam R. S. and Romaniec, Marek P.M. and Hazlewood, Geoffrey P. and Freedman, Robert B. (1995) Characterization of the Subunits in an Apparently Homogeneous Subpopulation of Clostridium-Thermocellum Cellulosames. Enzyme and Microbial Technology, 17 (8). pp. 705-711. ISSN 0141-0229. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1016/0141-0229(94)00118-B

Abstract

Clostridium thermocellum cellulosomes isolated by cellulose affinity chromatography were fractionated by anion exchange chromatography into apparently homogeneous subpopulations that differed with respect to enzyme activity and subunit composition. One such subpopulation contained predominantly six subunits and was closely similar to the ''subcellulosome'' described by Kobayashi et al. (Kobayashi, T., Romaniec, M. P. M., Fauth, U., and Demain, A. L., Appl. Environ. Microbiol., 1990, 56, 3040-3046). Avicelase specific activity of this homogeneous subpopulation was slightly higher than that of unfractionated cellulosomes, but the two preparations were similarly affected by Ca2+, dithiothreitol, and cellobiose. Determination of their N-terminal sequences and enzyme activities has enabled three of the six major subunits of the subpopulation of cellulosomes to be positively identified as known components of the C. thermocellum cellulase complex; the other three subunits did nor match up with previously characterized cellulosomal proteins.

Item Type: Article
Uncontrolled keywords: CLOSTRIDIUM THERMOCELLUM; CELLULOSOMES; CELLULOSE HYDROLYSIS
Subjects: T Technology > T Technology (General)
Divisions: Faculties > Science Technology and Medical Studies > School of Engineering and Digital Arts
Depositing User: P. Ogbuji
Date Deposited: 09 Jun 2009 09:31
Last Modified: 13 Jun 2014 10:36
Resource URI: http://kar.kent.ac.uk/id/eprint/19661 (The current URI for this page, for reference purposes)
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