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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)
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