Properties of a genetically reconstructed Prevotella ruminicola endoglucanase

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

Research output: Contribution to journalArticle

44 Citations (Scopus)

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 - 1992
Externally publishedYes

Fingerprint

Prevotella ruminicola
Cellulase
endo-1,4-beta-glucanase
Cellulose
cellulose
Thermobifida fusca
Cellulases
Carboxymethylcellulose Sodium
carboxymethylcellulose
enzyme
synergism
Enzymes
enzymes
plasmids
Plasmids
plasmid
degradation
filter
carboxymethylcellulase

ASJC Scopus subject areas

  • Biotechnology
  • Environmental Science(all)
  • Microbiology

Cite this

Properties of a genetically reconstructed Prevotella ruminicola endoglucanase. / Maglione, G.; Matsushita, Osamu; Russell, J. B.; Wilson, D. B.

In: Applied and Environmental Microbiology, Vol. 58, No. 11, 1992, p. 3593-3597.

Research output: Contribution to journalArticle

Maglione, G. ; Matsushita, Osamu ; Russell, J. B. ; Wilson, D. B. / Properties of a genetically reconstructed Prevotella ruminicola endoglucanase. In: Applied and Environmental Microbiology. 1992 ; Vol. 58, No. 11. pp. 3593-3597.
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