TAILIEUCHUNG - Báo cáo khoa học: Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai

A cellulase [endo-b-1,4-D-glucanase (EC )] was iso-lated from the hepatopancreas of abalone Haliotis discus hannaiby successive chromatographies on TOYOPEARL CM-650M, hydroxyapatite and Sephacryl S-200 HR. The molecular mass of the cellulase was estimated to be 66 000 Da by SDS/PAGE, thus the enzyme was named HdEG66. The hydrolytic activity of HdEG66 toward carb-oxymethylcellulose showed optimal temperature and pH at 38 Cand , respectively. | Eur. J. Biochem. 270 771-778 2003 FEBS 2003 doi Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai Ken-ichi Suzuki Takao Ojima and Kiyoyoshi Nishita Laboratory of Biochemistry and Biotechnology Graduate School of Fisheries Sciences Hokkaido University Japan A cellulase endo-b-1 4-D-glucanase EC was isolated from the hepatopancreas of abalone Haliotis discus hannai by successive chromatographies on TOYOPEARL CM-650M hydroxyapatite and Sephacryl S-200 HR. The molecular mass of the cellulase was estimated to be 66 000 Da by SDS PAGE thus the enzyme was named HdEG66. The hydrolytic activity of HdEG66 toward carboxymethylcellulose showed optimal temperature and pH at 38 C and respectively. cDNAs encoding HdEG66 were amplified by the polymerase chain reaction from an abalone hepatopancreas cDNA library with primers synthesized on the basis of partial amino-acid sequences of HdEG66. By overlapping the nucleotide sequences of the cDNAs a sequence of 1898 bp in total was determined. The coding region of 1785 bp located at nucleotide position 56-1840 gave an amino-acid sequence of 594 residues including the initiation methionine. The N-terminal region of 14 residues in the deduced sequence was regarded as the signal peptide as it was absent in HdEG66 protein and showed high similarity to the consensus sequence for signal peptides of eukaryote secretory proteins. Thus matured HdEG66 was thought to consist of 579 residues. The C-terminal region of453 residues in HdEG66 . approximately the C-terminal three quarters of the protein showed 42-44 identity to the catalytic domains of glycoside hydrolase family 9 GHF9 -cellulases from arthropods and Thermomonospora fusca. While the N-terminal first quarter of HdEG66 showed 27 identity to the carbohydrate-binding module CBM of a Cellulomonas fimi cellulase CenA. Thus the HdEG66 was regarded as the GHF9-cellulase possessing a family II CBM in the N-ter-minal

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