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Purification and properties of two truncated endoglucanases produced in Escherichia coli harbouring Clostridium cellulolyticum endoglucanase gene celCCD
- Source :
- Applied Microbiology and Biotechnology; March 1993, Vol. 38 Issue: 6 p750-754, 5p
- Publication Year :
- 1993
-
Abstract
- The endoglucanase gene, celCCD, of Clostridium cellulolyticum has been expressed in Escherichia coli. Multiple active polypeptides were detected in the E. coli cells. The relative molecular mass (M<subscript>r</subscript>) of two major active polypeptides were 56 000 (D56) and 38 000 (D38), which were smaller than the deduced M<subscript>r</subscript> of the mature protein (63 401). D56 and D38 were purified from the periplasmic fraction. The N-terminal sequences of the two purified polypeptides were identical to that of the mature endoglucanase (Ala-Ile-Asn-Ser-Gln-Asp-Met-Val---) deduced from the nucleotide sequence. These data indicated that these polypeptides were produced by processing the original mature protein in the C-terminal region. The enzymatic properties of these two polypeptides were very similar, except that the specific activity of D38 was 2–3.5-fold higher than that of D56, and D38 was more heat stable than D56.
Details
- Language :
- English
- ISSN :
- 01757598 and 14320614
- Volume :
- 38
- Issue :
- 6
- Database :
- Supplemental Index
- Journal :
- Applied Microbiology and Biotechnology
- Publication Type :
- Periodical
- Accession number :
- ejs15713535
- Full Text :
- https://doi.org/10.1007/BF00167140