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Purification and characterization of a new endoglucanase from Aspergillus aculeatus.
Naika, Gajendra Sunnamada and Kaul, Purnima and Prakash, V. (2007) Purification and characterization of a new endoglucanase from Aspergillus aculeatus. Journal of agricultural and food chemistry, 55 (18). pp. 7566-72. ISSN 0021-8561
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Abstract
Endoglucanase has been isolated from Aspergillus aculeatus. The purified enzyme showed a single band and had a molecular weight of 45,000 Da as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with a specific activity of 1.4 units/mg. The purified enzyme was identified as endoglucanase, showing a high specific activity toward CM-cellulose and low specific activity toward Avicel. The activity of the isolated enzyme was optimum at a pH of 5.0 and temperature of 40 degrees C, respectively. The isoelectric point of the enzyme was 4.3. T(m) was found to be 57 degrees C. The treatment of the endoglucanase with diethylpyrocarbonate resulted in the modification of the histidine residues present in the enzyme, with a concomitant loss of 70% of the original enzymatic activity. However, carbodiimide completely inactivated the endoglucanase. The results show that the enzyme is able to sustain 50% of its activity even when heated at 90 degrees C for a period of 5 h. Endoglucanase can be used in the controlled hydrolysis of cellulose and other cellulose-rich foods. It can be used in the development of targeted functional foods from agrimaterials for value addition in the food chain.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Aspergillus aculeatus; activity; CM-cellulose; carbodiimide; endoglucanase |
| Subjects: | 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes |
| Divisions: | Protein Chemistry and Technology |
| Depositing User: | Food Sci. & Technol. Information Services |
| Date Deposited: | 07 Aug 2008 11:21 |
| Last Modified: | 28 Dec 2011 09:35 |
| URI: | http://ir.cftri.res.in/id/eprint/1847 |
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