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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F11%3A10107200%21RIV12-GA0-11310___
rdf:type
skos:Concept n8:Vysledek
rdfs:seeAlso
http://www.nel.edu
dcterms:description
Comamonas testosteroni Pb50 is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This bacterial strain is capable of utilizing phenol as the sole carbon and energy source. Although examples are known in which the C. testosteroni utilizes phenol for growth or metabolism, much less information are known on the nature of the phenol-oxidizing enzymes in this microorganism. Therefore, the occurrence and cellular location of phenol hydroxylase (EC 1.14.13.7), the enzyme participating in the first step of phenol degradation, catalyzing its hydroxylation to catechol in a bacterial Comamonas testosteroni Pb50 strain grown in the presence of phenol as a sole carbon and energy source are the aims of this study. Comamonas testosteroni Pb50 is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This bacterial strain is capable of utilizing phenol as the sole carbon and energy source. Although examples are known in which the C. testosteroni utilizes phenol for growth or metabolism, much less information are known on the nature of the phenol-oxidizing enzymes in this microorganism. Therefore, the occurrence and cellular location of phenol hydroxylase (EC 1.14.13.7), the enzyme participating in the first step of phenol degradation, catalyzing its hydroxylation to catechol in a bacterial Comamonas testosteroni Pb50 strain grown in the presence of phenol as a sole carbon and energy source are the aims of this study.
dcterms:title
Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni
skos:prefLabel
Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni
skos:notation
RIV/00216208:11310/11:10107200!RIV12-GA0-11310___
n8:predkladatel
n9:orjk%3A11310
n4:aktivita
n7:Z n7:P
n4:aktivity
P(1M0505), P(GAP503/11/0163), Z(MSM0021620808)
n4:cisloPeriodika
Suppl. 1
n4:dodaniDat
n15:2012
n4:domaciTvurceVysledku
n5:8309590 n5:6850243 n5:8486573 n5:1631071 n5:5356504
n4:druhVysledku
n16:J
n4:duvernostUdaju
n14:S
n4:entitaPredkladatele
n11:predkladatel
n4:idSjednocenehoVysledku
205913
n4:idVysledku
RIV/00216208:11310/11:10107200
n4:jazykVysledku
n20:eng
n4:klicovaSlova
phenol hydroxylase; Comamonas testosteroni; biodegradation; phenol
n4:klicoveSlovo
n6:phenol%20hydroxylase n6:Comamonas%20testosteroni n6:biodegradation n6:phenol
n4:kodStatuVydavatele
SE - Švédské království
n4:kontrolniKodProRIV
[A4B9B05CF6FB]
n4:nazevZdroje
Neuroendocrinology Letters
n4:obor
n21:CE
n4:pocetDomacichTvurcuVysledku
5
n4:pocetTvurcuVysledku
7
n4:projekt
n10:GAP503%2F11%2F0163 n10:1M0505
n4:rokUplatneniVysledku
n15:2011
n4:svazekPeriodika
32
n4:tvurceVysledku
Vilímková, Lenka Stiborová, Marie Halecký, Martin Kremláčková, Veronika Turek, Michal Páca, Jan
n4:zamer
n19:MSM0021620808
s:issn
0172-780X
s:numberOfPages
9
n18:organizacniJednotka
11310