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Applied and Environmental Microbiology, January 2002, p. 430-433, Vol. 68, No. 1
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.1.430-433.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Hyperthermostable Endoglucanase from Pyrococcus horikoshii

Susumu Ando,1,2* Hiroyasu Ishida,3 Yoshitsugu Kosugi,3 and Kazuhiko Ishikawa1*

National Institute of Advanced Industrial Science and Technology (Kansai), Ikeda, Osaka 563-8577,1 Rakuto Kasei Industrial Co. Inc., Otsu, Shiga 520-2277,2 National Institute of Advanced Industrial Science and Technology (Tsukuba), Tsukuba, Ibaraki 305-8566, Japan3

Received 25 June 2001/ Accepted 25 October 2001

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 ß-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.

* Corresponding author. Mailing address: Special Division for Human Life Technology, National Institute of Advanced Industrial Science and Technology (Kansai), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan. Phone: 81-727-51-9526. Fax: 81-727-51-9628. E-mail for Susumu Ando: andosusumu{at}hotmail.com. E-mail for Kazuhiko Ishikawa: kazu-ishikawa{at}aist.go.jp.

Applied and Environmental Microbiology, January 2002, p. 430-433, Vol. 68, No. 1
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.1.430-433.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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