ABSTRACT
An endoglucanase homolog from the hyperthermophilic archaeon
Pyrococcus horikoshii
was expressed in
Escherichia coli
, and its enzymatic characteristics were examined. The expressed protein was a hyperthermostable endoglucanase which hydrolyzes celluloses, including Avicel and carboxymethyl cellulose, as well as β-glucose oligomers. This enzyme is the first endoglucanase belonging to glycosidase family 5 found from
Pyrococcus
species and is also the first hyperthermostable endoglucanase to which celluloses are the best substrates. This enzyme is expected to be useful for industrial hydrolysis of cellulose at high temperatures, particularly in biopolishing of cotton products.
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