Purification and characterization of a new endoglucanase from Aspergillus aculeatus

Naika, Gajendra Sunnamada ; Kaul, Purnima ; Prakash, Vishweshwaraiah (2007) Purification and characterization of a new endoglucanase from Aspergillus aculeatus Journal of Agricultural and Food Chemistry, 55 (18). pp. 7566-7572. ISSN 0021-8561

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Official URL: http://pubs.acs.org/doi/abs/10.1021/jf070710p

Related URL: http://dx.doi.org/10.1021/jf070710p

Abstract

Endoglucanase has been isolated from Aspergillus aculeatus. The purified enzyme showed a single band and had a molecular weight of 45000 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°C, respectively. The isoelectric point of the enzyme was 4.3. Tm was found to be 57°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°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
Source:Copyright of this article belongs to American Chemical Society.
Keywords:Aspergillus aculeatus; Activity; CM-cellulose; Carbodiimide; Endoglucanase
ID Code:38681
Deposited On:03 May 2011 07:54
Last Modified:03 May 2011 07:54

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