Aqueous extracts of homogenized shoot and root tissue of alfalfa
(Medicago sativa L.), white mustard (Sinapis alba
L.), and cress (Lepidium sativum L.), with the exudates of sterile
roots of these crop plants, were examined
spectrophotometrically for the activities of 20 oxidoreductase enzymes
by
standard procedures. In tissue extracts
and root exudates, the reactions of laccase (EC 1.10.3.2), ascorbate oxidase
(EC 1.10.3.3), monophenol monooxygenase (EC 1.14.18.1), and phenol 2-monooxygenase
(EC 1.14.13.7) were readily detected. Of the
aromatic-ring cleavage dioxygenases, those of the meta-cleavage pathway
(EC 1.13.11.2 and 1.13.11.8) could
also be detected. Guaiacol peroxidase (EC 1.11.1.7) was dominant in
all samples. In sterile root exudates of
alfalfa, this enzyme was represented by at least seven acidic isoforms.
The
formation of the ligninolytic Mn3+/malonate and Mn3+/citrate
complexes from Mn2+ occurred in all tissue extracts and in root
exudates of
alfalfa. In root extracts of soybean (Glycinemax L.), the rate
of Mn3+
generation correlated (P=0·993) with the
activities of endogenous plant guaiacol peroxidase and horseradish peroxidase
(HRP) supplements and also with
the total phenol content in tissue extracts (P=0·984).
Plant
guaiacol peroxidase and purified HRP decolorized
four aromatic dyes, an activity reported to be involved in ligninolysis.
Although no enzymes capable of generating
H2O2 as a consequence of the oxidation of simple
sugars, amino acids, organic acids, and aldehydes were found,
traces of peroxide were detected in tissue extracts and in the root exudate
of alfalfa. It is concluded that the
oxidoreductases found in plant tissues also occur in root exudates of
aseptic whole plants. The significance of
interrelations between oxidoreductase enzymes and enzymically generated
higher-valency metal ions is discussed
in the context of the oxidative conversion of phenolic compounds in soil
and plant tissue.