Báo cáo khoa học: A thermoacidophilic endoglucanase (CelB) fromAlicyclobacillus acidocaldariusdisplays high sequence similarity to arabinofuranosidases belonging to family 51 of glycoside hydrolases
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A100-kDa proteinwith endoglucanase activitywas purifiedfrom Triton X-100 extract of cells of the thermoacidophilicGram-positive bacterium Alicyclobacillus acidocaldarius.The enzyme exhibited activity towards carboxy methyl cel-lulose and oat spelt xylan with pH and temperature optimaof 4 and 80C, respectively. Cloning and nucleotidesequence analysis of the corresponding gene (celB) revealedan ORF encoding a preprotein of 959 amino acids whichis consistent with an extracellular localization. Purifiedrecombinant CelB and a variant lacking the C-terminal 203amino acid residues (CelBtrunc) displayed similar enzymaticproperties as the wild-type protein. Analysis of productformation suggested an endo mode of action. ...
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Báo cáo khoa học: A thermoacidophilic endoglucanase (CelB) fromAlicyclobacillus acidocaldariusdisplays high sequence similarity to arabinofuranosidases belonging to family 51 of glycoside hydrolases
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: A thermoacidophilic endoglucanase (CelB) fromAlicyclobacillus acidocaldariusdisplays high sequence similarity to arabinofuranosidases belonging to family 51 of glycoside hydrolases
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