Hyperthermostable endoglucanase from Pyrococcus horikoshii.
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 beta-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.
Ando
Susumu
S
National Institute of Advanced Industrial Science and Technology, Kansai, Ikeda, Osaka 563-8577, Japan. andosusumu@hotmail.com
Ishida
Hiroyasu
H
Kosugi
Yoshitsugu
Y
Ishikawa
Kazuhiko
K
D000595:Amino Acid Sequence; D002480:Cellulase / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006358:Hot Temperature; D008969:Molecular Sequence Data; D019711:Pyrococcus / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017422:Sequence Analysis, DNA
D011994:Recombinant Proteins; D002482:Cellulose; D002480:Cellulase