Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 53:759-763 (1974)
© 1974 American Society of Plant Biologists

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 Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (20)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sobotka, F. E.
Right arrow Articles by Stelzig, D. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sobotka, F. E.
Right arrow Articles by Stelzig, D. A.
Agricola
Right arrow Articles by Sobotka, F. E.
Right arrow Articles by Stelzig, D. A.
Articles

An Apparent Cellulase Complex in Tomato (Lycopersicon esculentum L.) Fruit 1

Francis E. Sobotka2 and David A. Stelzig

a Division of Plant Sciences, West Virginia University, Morgantown, West Virginia 26506

Four enzyme-containing fractions were separated by ammonium sulfate fractionation of 2-day, postbreaker tomato (Lycopersicon esculentum L. cv. Manhattan). The pH optima and substrate specificities are reported. The enzymes were identified as a nonspecific {beta}-glucosidase, an exo-{beta}-1,4-glucanase, and two endocellulases. Both endocellulase fractions were able to catalyze the hydrolysis of various insoluble cellulose materials.

Together, the enzymes studies are capable of completely degrading insoluble cellulose to short chain cellodextrins and glucose. Ripening tomato fruit apears to contain a complex of cellulases similar to that of cellulolytic bacteria and fungi.


2 Present address: Research and Development, Hunt Wesson Foods, Inc., P. O. Box 107, Perrysburg, Ohio 43551.

1 Manuscript published with the approval of the Director of the West Virginia Agricultural Experiment Station, Morgantown, as Scientific Paper No. 1281.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1974 by the American Society of Plant Biologists