Purification and characterization of an endoglucanase from the marine rotifer, Brachionus plicatilis
| Autor: | Young Tae Kim, Chang Zoon Chun, Sung Bum Hur |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Clinical Biochemistry
Rotifera Rotifer Cellulase Biochemistry Microbiology Hydrolysis chemistry.chemical_compound Cellulose 1 4-beta-Cellobiosidase Genetics Animals Cellulose Molecular Biology Gel electrophoresis Chromatography biology beta-Glucosidase Temperature Cell Biology Hydrogen-Ion Concentration Glucanase Brachionus biology.organism_classification Molecular Weight Chlorella Durapatite chemistry Carboxymethylcellulose Sodium Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel |
| Zdroj: | IUBMB Life. 43:241-249 |
| ISSN: | 1521-6543 |
| DOI: | 10.1080/15216549700204021 |
| Popis: | The marine rotifer, Brachionus plicatilis, is able to digest Chlorella efficiently, suggesting that the rotifer contains a powerful cellulolytic enzyme system. A multi-component cellulolytic complex, including endoglucanase (CM-cellulase), cellobiohydrolase and beta-glucosidase, was found in Brachionus plicatilis. Endoglucanase (endo-beta-1,4 glucanase) was purified to homogeneity from rotifer homogenates using a sequential chromatographic method. The purified enzyme exhibits a strong hydrolytic activity with carboxymethyl(CM)-cellulose. The optimum temperature and pH for the endoglucanase activity were 37 degrees C and 7.0, respectively. 80% of the CM-cellulase activity was retained in salt mixture that ranged from 150 to 500 mM NaCl equivalent. The purified protein was isolated with a molecular weight of approximately 62 kDa estimated by SDS-polyacrylamide gel electrophoresis. |
| Databáze: | OpenAIRE |
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