Aim of this work was to find the best source for obtaining high amount
of copper amine oxidase (EC 1.4.3.6) that can be further used for ana
lytical or industrial applications. The study focused on plant enzymes
, because they occur in much higher content in the starting material t
han the enzymes from other sources, have higher specific activity and
are also more thermostable. Presence of the amine oxidase was tested i
n extracts from 4 to 7-d-old seedlings of thirty-four various Fabaceae
plants. Amine oxidases hom nine selected plants were purified by gene
ral method involving ammonium sulfate fractionation, controlled heat d
enaturation, and three chromatographic steps. Kinetic properties of th
e amine oxidases purified were tested with a wide range of substrates
and inhibitors and were found to be very similar. Best purification yi
eld, and total and specific activities were obtained for the enzyme fr
om grass pea (Lathyrus sativus) throughout all purification steps. Hen
ce, the grass pea extract was chosen as a suitable candidate for massi
ve production of the amine oxidase.