Properties of a genetically reconstructed Prevotella ruminicola endoglucanase

G. Maglione, O. Matsushita, J. B. Russell, D. B. Wilson

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Abstract

A pUC19-derived plasmid was constructed that coded for a hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40.5-kDa carboxymethyl cellulase (CMCase). The hybrid enzyme was purified and characterized enzymatically. It bound tightly to cellulose, and its specific activities on carboxymethyl cellulose, amorphous cellulose, and ball-milled cellulose were 1.5, 10, and 8 times that of the 40.5-kDa CMCase, respectively. Furthermore, the modified enzyme gave synergism with an exocellulase in the degradation of filter paper, while the 40.5-kDa CMCase did not.

Original languageEnglish
Pages (from-to)3593-3597
Number of pages5
JournalApplied and environmental microbiology
Volume58
Issue number11
Publication statusPublished - Jan 1 1992
Externally publishedYes

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ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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