A β-1,4-endoglucanase-encoding gene from Cellulomonas pachnodae |
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| Authors: | A E Cazemier J C Verdoes H J M Op den Camp J H P Hackstein A J J van Ooyen |
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| Institution: | (1) Department of Microbiology and Evolutionary Biology, Faculty of Science, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands e-mail: huubcamp@sci.kun.nl Tel.: +31-24-3652657 Fax: +31-24-3652830, NL;(2) Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen University and Research Center, P.O. Box 8129, 6700 EV Wageningen, The Netherlands, NL |
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| Abstract: | A gene library of Cellulomonas pachnodae was constructed in Escherichia coli and was screened for endoglucanase activity. Five endoglucanase-positive clones were isolated that carried identical DNA
fragments. The gene, designated cel6A, encoding an endoglucanase enzyme, belongs to the glycosyl hydrolase family 6 (cellulase family B). The recombinant Cel6A
had a molecular mass of 53 kDa, a pH optimum of 5.5, and a temperature optimum of 50–55 °C. The recombinant endoglucanase
Cel6A bound to crystalline cellulose and beech litter. Based on amino acid sequence similarity, a clear cellulose-binding
domain was not distinguished. However, the regions in the Cel6A amino acid sequence at the positions 262–319 and 448–473,
which did not show similarity to any of the known family-6 glycosyl hydrolases, may be involved in substrate binding.
Received: 14 January 1999 / Received revision: 29 March 1999 / Accepted: 6 April 1999 |
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