Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hatfield, R.
Right arrow Articles by Nevins, D. J.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Hatfield, R.
Right arrow Articles by Nevins, D. J.
Agricola
Right arrow Articles by Hatfield, R.
Right arrow Articles by Nevins, D. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1986, Vol. 27, No. 3 541-552
© 1986

Article

Characterization of the Hydrolytic Activity of Avocado Cellulase1

Ronald Hatfield2 and Donald J. Nevins3,4

Botany Department, Iowa State University Ames, 1A 50011, U.S.A.

4Author to whom correspondence should be addressed.

The cellulase produced by ripening avocado fruits (Persea americana Mill cv. Fuerte) was isolated and purified using chromatofocusing (pH 7–4) and gel filtration on a Bio- Gel P-100 column. Characteristics of the cellulase were assessed by using, as substrates, a range of polysaccharides containing various sugar residues and varying types of linkages between the residues. Only those substrates containing (1->4)-ß-glucosyl linkages were hydrolyzed by the purified enzyme. Two polysaccharides that were extensively hydrolyzed by the cellulase were carboxymethylcellulose and (1->3),(1->4)-ß-D-glucans such as from Avena endosperm cell walls. Characterization of the activity in the degradation of the mixed linked glucan of Avena and cellodextrins indicated that the enzyme has a limit recognition-hydrolytic site of four (l->4)-ß linked glucose residues. It was also found that the enzyme could cleave only (1->4)-ß-linkages that were adjacent to other (l->4)-ß-D-glucosyl linkages. Activity of the cellulase against isolated avocado fruit cell walls indicated that the purified enzyme was incapable of appreciably solubilizing the cellulosic components of these walls.

1Supported in part by National Science Foundation Research Grant PCM 7818588.

2USDA-ARS, Dairy Forage Research Center, University of Wisconsin, Madison, WI 53706.

3Department of Vegetable Crops, University of California, Davis, CA 95616.

(Received September 14, 1985; Accepted February 12, 1986)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J Exp BotHome page
K. Hiwasa, Y. Kinugasa, S. Amano, A. Hashimoto, R. Nakano, A. Inaba, and Y. Kubo
Ethylene is required for both the initiation and progression of softening in pear (Pyrus communis L.) fruit
J. Exp. Bot., February 1, 2003; 54(383): 771 - 779.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. H. Harpster, D. A. Brummell, and P. Dunsmuir
Expression Analysis of a Ripening-Specific, Auxin-Repressed Endo-1,4-beta -Glucanase Gene in Strawberry
Plant Physiology, December 1, 1998; 118(4): 1307 - 1316.
[Abstract] [Full Text]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.