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ABSTRACT: Background
The archeaon Sulfolobus solfataricus P2 encodes a thermoacidophilic cellulase which shows an extreme acid and thermal stability with a pH optimum at 1.8 and a temperature optimum at 80°C. This extraordinary enzyme could be useful for biotechnological exploitation but the expression and purification in expression hosts like E. coli is unsatisfactory due to the high aggregation tendency of the recombinant enzyme. The thermophilic cellulase CelA from Thermotoga maritima belongs to the same glycoside hydrolase family (GH12) but has a neutral pH optimum. In contrast to SSO1949 this enzyme is expressed partially soluble in E. coli.Results
We aimed to constructed a hybrid enzyme based on these two beta-endoglucanases which should successfully combine the advantageous pr
SUBMITTER: Kufner K
PROVIDER: S-EPMC3655044 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature