An Endoglucanase, EglA, from the Hyperthermophilic Archaeon Pyrococcus furiosus Hydrolyzes β-1,4 Bonds in Mixed-Linkage (1→3),(1→4)-β- d -Glucans and Cellulose

Volume: 181, Issue: 1, Pages: 284 - 290
Published: Jan 1, 1999
Abstract
The eglA gene, encoding a thermostable endoglucanase from the hyperthermophilic archaeon Pyrococcus furiosus , was cloned and expressed in Escherichia coli . The nucleotide sequence of the gene predicts a 319-amino-acid protein with a calculated molecular mass of 35.9 kDa. The endoglucanase has a 19-amino-acid signal peptide but not cellulose-binding domain. The P. furiosus endoglucanase has significant amino acid sequence similarities,...
Paper Details
Title
An Endoglucanase, EglA, from the Hyperthermophilic Archaeon Pyrococcus furiosus Hydrolyzes β-1,4 Bonds in Mixed-Linkage (1→3),(1→4)-β- d -Glucans and Cellulose
Published Date
Jan 1, 1999
Volume
181
Issue
1
Pages
284 - 290
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