Purification, characterization and cloning of an endo-1,4-B-glucanase fromRuminococcus sp.

Abstract

Endoglucanase ofRuminococcus sp. is composed of seven active protein components when chromatographed on an ion exchange column (Q-Sepharose). Component I (endoglucanase A) did not bind to the column and was purified to homogeneity by molecular sieve chromatography. It had a mol. wt. of 22 000. Component II was fractionated into two active protein peaks (endoglucanase B and C) having mol. wt. of 225 000 and 10 000. The endoglucanase A had high affinity for CMC (Km 8 mg/ml). The temperature optimum of all three endoglucanase was between 40–45°C. The gene encoding for endolucanase activity was cloned inE. coli HB101 with pBR322. A 4.3 kilobaseBamH1 fragment encoding endoglucanase was hybridized toRuminococcus chromosomal DNA.

DOI: 10.1007/BF01022097

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Cite this paper

@article{Srivastava2005PurificationCA, title={Purification, characterization and cloning of an endo-1,4-B-glucanase fromRuminococcus sp.}, author={Sudeep Kumar Srivastava and Arif Ali and Sunil S Khanna}, journal={Biotechnology Letters}, year={2005}, volume={13}, pages={907-912} }