Extraction and partial characterization of the ethylene-forming enzyme from apple fruit

• Published in: Plant physiology (Bethesda) Vol. 99; no. 2; pp. 751 - 754
• Main Authors: Fernandez-Maculet, J.C. (University of California, Davis, CA), Yang, S.F
• Format: Journal Article
• Language: English
• Published: United States American Society of Plant Physiologists 01.06.1992
• Subjects: 1-amino cyclopropane-1-carboxylic acid; ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; alpha -aminoisobutyric acid; characterization; Cobalt; Communications; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; Cytosol; ENZIMAS; ENZYME; Enzyme activity; Enzymes; ETHYLENE; Ethylene production; ethylene-forming enzyme; ETILENO; FRUITS; FRUTAS; inhibitor; MADURAMIENTO; Malus domestica; MALUS PUMILA; MURISSAGE; Norepinephrine; Oxygen; Plants; PRODUCCION VEGETAL; PRODUCTION VEGETALE; PURIFICACION; PURIFICATION; Vacuoles
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.99.2.751

Ethylene-forming enzyme (EFE) was isolated from apple (Malus domestica Borkh. cv Golden Delicious) fruit tissue. The enzyme activity in the homogenate is associated with the pellet fraction and can be solubilized with Triton X-100 or polyvinylpolypyrrolidone. The solubilized enzyme system resembles the in vivo system in that it exhibits a low Km (17 micromolar) for its substrate 1-aminocyclopropane-1-carboxylic acid (ACC), is stereospecific toward 2-ethyl-ACC stereoisomers for 1-butene production, and is inhibited by cobalt ions and alpha-aminoisobutyric acid. Intact preclimacteric fruits treated with exogenous ethylene showed a marked increase in in vivo EFE activity and this increase was accompanied by a parallel increase in in vitro EFE activity. These results support the notion that the isolated EFE represents the authentic in vivo activity