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Extraction and biochemical characterization of 1‐aminocyclopropane‐1‐carboxylic acid oxidase from pear
Author(s) -
Vioque Blanca,
Castellano José María
Publication year - 1994
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1994.tb00396.x
Subject(s) - pear , pyrus communis , chemistry , oxidase test , enzyme , 1 aminocyclopropane 1 carboxylic acid , stereochemistry , biochemistry , botany , biosynthesis , biology
Activity and biochemical characteristic of 1‐aminocyclopropane‐1‐carboxylic acid (ACC) oxidase from pear ( Pyrus communis cv. Blanquilla) was determined. The enzyme showed a low K m (57.5 μM) for ACC and was dependent on O 2 (K m 0.44% in atmosphere). It had an absolute requirement for Fe 2+ , ascorbate and CO 2 and was inhibited by α‐aminoisobutyric acid (AIB: K 1 4.2 m M ) and cobalt. ACC oxidase has an optimum pH of 6.7 and temperature maxima at 28 and 38°C and it is concluded that the activity of ACC oxidase from pear resembles authentic in vivo activity.