Abstract
A Clostridium cellulovorans lambda gt1l gene bank was screened for endo-1,4-β-glucanase [EC 3.2.1.4, EGase, Carboxy Methyl Cellulase (CMCase)] genes using a chromogenic substrate. Three genes (engA, engB, and engC) were isolated. The engB expressed the most active CMCase. The engA encoded a bifunctional enzyme that displayed endo-1,4-β-glucanase and β-glucosidase activities. The three recombinant glucanases, when expressed in Escherichia coli, were partially degraded into multiform active enzymes as evidenced by their SDS-PAGE-CMC zymograms. None of the clones could degrade crystalline cellulose, thus supporting the hypothesis that the integrity of the C. cellulovorans cellulase complex was essential for its 'true cellulase' activity.
| Original language | English |
|---|---|
| Pages (from-to) | 667-672 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 169 |
| Issue number | 2 |
| DOIs | |
| State | Published - 15 Jun 1990 |
| Externally published | Yes |
Bibliographical note
Funding Information:ACKNOWLEDGMENWTSe: thank Reinhold Bruckner for his suggestions on the cloning strategy. O.S. was supported by fellowship SI-0057-87 from The United State-Israel Binational Agricultural Research and Development Fund. The research was supported in part by Department of Energy grant #DE-FG03-87FR13705( RHD).