Purification, characterization and structural analysis of an abundant β-1,3-glucanase from banana fruit
Article first published online: 25 DEC 2001
DOI: 10.1046/j.1432-1327.2000.01117.x
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How to Cite
Peumans, W. J., Barre, A., Derycke, V., Rougé, P., Zhang, W., May, G. D., Delcour, J. A., Van Leuven, F. and Van Damme, E. J. M. (2000), Purification, characterization and structural analysis of an abundant β-1,3-glucanase from banana fruit. European Journal of Biochemistry, 267: 1188–1195. doi: 10.1046/j.1432-1327.2000.01117.x
Publication History
- Issue published online: 25 DEC 2001
- Article first published online: 25 DEC 2001
- (Received 2 November 1999, revised 16 December 1999, accepted 21 December 1999)
- Abstract
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Keywords:
- banana;
- β-1;
- 3-glucanase;
- Musa;
- PR protein
An abundant, catalytically active β-1,3-endoglucanase (EC 3.2.1.39) has been isolated from the pulp of ripe bananas. Biochemical analysis of the purified protein, molecular modelling, and molecular cloning of the corresponding gene indicate that this banana enzyme closely resembles previously characterized plant β-glucanases with respect to its amino-acid sequence, structure and biological activity. The results described in this paper demonstrate both the occurrence of an abundant active β-1,3-endoglucanases in fruits and also readdress the question of the possible involvement of these enzymes in the ripening and/or softening process.

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