No
studies
on
degradation
of
lignin,
dyes
and
aromatic
pollu-
tants
using
peroxidase
activity
of
Prx
have
been
reported
so
far,
but
many
typical
hemoperoxidase,
including
horseradish
peroxi-
dase,
soybean
peroxidase,
lignin
(LiP)
peroxidase
and
manganese
(MnP)
peroxidase,
had
been
widely
applied
in
clinical
analysis,
decolorization
in
paper
and
textile
industries,
and
decontaminated
of
aromatic
pollutants.
ZEN
is
somewhat
structurally
related
to
the
above-mentioned
aromatic
pollutants
(
Fig.
1
).
However,
not
many
works
have
been
reported
on
the
degradation
of
ZEN
by
these
per-
oxidases
(
Peter
2000;
Ogawaa
et
al.
2004;
Zinedinea
et
al.
2007
).
To
further
conform
whether
Prx
identified
on
the
previous
find-
ings
(
Yu
et
al.
2011
)
was
involved
to
ZEN
degradation,
a
gene
of
Prx
from
Acinetobacter
sp.
SM04
was
cloned
and
expressed
in
E.
coli
BL2
(DE3).
Meanwhile,
the
activity
of
recombinant
Prx
to
degrade
ZEN
was
also
assessed.
2.