Nucleotide sequence of gene celM encoding a new endoglucanase (CeIM) of Clostridium thermocellum and purification of the enzyme

Autor: Ulf T. Gerngross, Arnold L. Demain, Patrick J. Barker, T. Kobayashi, M.P.M. Romaniec
Rok vydání: 1993
Předmět:
Zdroj: Journal of Fermentation and Bioengineering. 76:251-256
ISSN: 0922-338X
DOI: 10.1016/0922-338x(93)90189-f
Popis: The nucleotide sequence of a new endoglucanase gene ( celM ) of Clostridium thermocellum was determined. The structural gene contains an open reading frame of 978 by starting with an ATG codon and terminating in a TGA stop codon. The deduced amino acid sequence of endoglucanase M (CeIM) contains 325 amino acids (MW 35,186) and its N-terminal amino acid sequence is identical to that of the purified enzyme. The codon usage of the gene is similar to that of other endoglucanase genes in the same organism. The endoglucanase was purified from Escherichia coli with a 200-fold increase in specific activity. The optimum pH and temperature values of the enzyme are 5.5 to 6.5 and 60°C respectively for carboxymethylcellulose (CMC) degradation.
Databáze: OpenAIRE