p monooxygenase family. So, this enzyme catalyzes the

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Therefore,
it seems that this strain converts benzene to phenol in the
degradation route. Furthermore,
neither
styrene
dioxygenase
nor cis-1,2-dihydrobenzene-1,2-diol
dehydrogenase,
enzymes
related to oxidize styrene to 3-Vinylcatechol (6057),
were not found
while
the
xylE,
xylF,
catA,
gctA,
gctB,
feaB
and
pct
genes
are present in the strain YKJ
genome (table
(S_Table
7)).
The
3-vinylcatechol degradation then progress further in two route, which
is oxidized to
either
pyruvate and acetaldehyde or
2-vinyl-cis,cis-muconate,
ultimately directing into
pyruvate metabolism or benzoate degradation route,
respectively
(6058). On
the other hand,
the
laboratory tests also revealed
that this strain is capable of growth on chlorobenzene, banzene and
styrene as only source of carbon and
energy (Figure S, R,O).
Due
to the considerable variety and specific functional properties,
monooxygenase enzymes are able to degrade various aromatic compounds
by aromatic ring cleavage. For
an instance, a novel phenol hydroxylase was identified in Bacillus
thermoglucosidasius A7,
belonging to flavin-dependant monooxygenase family. So, this enzyme
catalyzes the efficacious ortho-hydroxylation of phenol to catechol
while it’s activity is FAD-dependent (6061). As
reported by Mooney, Styrene
is generally metabolized through the oxidation of its side chain
under aerobic conditions. The scientific
reports plainly reveal a prevailing route for the side chain
oxidation of styrene. Accordingly, the
vinyl side chain oxidation is catalyzed via a FAD-dependent styrene
monooxygenase, leading to produce styrene epoxide (6020).
Other microorganisms, such as
Pseudomonas Pickettii, also use flavoprotein monooxygenases to
hydrolyze phenol. Therefore,
it can be concluded that the strain YKJ
is capable of decomposing
phenol,
bisphenol A, benzen, chlorobenzen, styrene, xylene and benzoic acid,
though
the isolate YKJ
are more tend to consume more phenol, bisphenol A and styrene.

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