Summary: An alkalophilic sp., no. 1139, was isolated from soil and this bacterium produced a carboxymethyl cellulase (CMCase). The production of enzyme was strongly inhibited by the addition of glucose. The CMCase was purified on a DEAE-Toyopearl 650 ion-exchange column followed by Toyopearl HW-55F gel filtration and passage through a DEAE-Toyopearl 650 ion-exchange column. The purified enzyme gave a single band of protein on PAGE. The enzyme hydrolysed carboxymethylcellulose with an optimum at pH 9.0 and a of 0.48 mg ml; no activity was observed at pH 6.0. The enzyme had a molecular weight (SDS-PAGE) of 92000 and an isoelectric point of 3.1. The maximum degree of hydrolysis of carboxymethylcellulose was about 30% and -glucosidase activity was also observed.


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