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 language | English |
|---|---|
| Pages (from-to) | 3593-3597 |
| Number of pages | 5 |
| Journal | Applied and Environmental Microbiology |
| Volume | 58 |
| Issue number | 11 |
| Publication status | Published - 1992 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biotechnology
- Environmental Science(all)
- Microbiology
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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 journal › Article
}
TY - JOUR
T1 - Properties of a genetically reconstructed Prevotella ruminicola endoglucanase
AU - Maglione, G.
AU - Matsushita, Osamu
AU - Russell, J. B.
AU - Wilson, D. B.
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026487255&partnerID=8YFLogxK
M3 - Article
C2 - 1482181
AN - SCOPUS:0026487255
VL - 58
SP - 3593
EP - 3597
JO - Applied and Environmental Microbiology
JF - Applied and Environmental Microbiology
SN - 0099-2240
IS - 11
ER -