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

Francis E. Sobotka | Zendy; David A. Stelzig | Zendy

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

Author(s) -

Francis E. Sobotka,

David A. Stelzig

Publication year - 1974

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.53.5.759

Subject(s) - lycopersicon , cellulase , cellulose , hydrolysis , enzyme , ammonium , chemistry , ripening , glucanase , fractionation , ammonium sulfate , substrate (aquarium) , biochemistry , botany , food science , biology , chromatography , organic chemistry , ecology

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.

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