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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F06%3A00039333%21RIV07-GA0-61388971
rdf:type
skos:Concept n12:Vysledek
dcterms:description
Celé buňky baktérie Rhodococcus equi A4, producenta nitrilhydratasy a amidasy, byly imobilizovány v čočkovitých částicích hydrogelu, LentiKats (R). Imobilizovaný biokatalyzátor byl použit pro biotransformaci benzonitrilu, 3-kyanopyridinu, (R,S)-3-hydroxy-2-methylenebutanenitrilu and (R,S)-3-hydroxy-2-methylene-3-phenylpropanenitrilu. Stabilita nitrilhydratasy během opakovaného použití biokatalyzátoru závisela na typu substrátu. Enzym byl stabilní během transformace (R,S)-3-hydroxy-2-methylenebutanenitrilu. Během reakce nebyla pozorována výraznější ztráta aktivity amidasy Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were immobilized in lens-shaped hydrogel particles. LentiKats (R). The immobilized biocatalyst was applied to the biotransformation of benzonitrile, 3-cyanopyridine, (R,S)-3-hydroxy-2-methylenebutanenitrile and (R,S)-3-hydroxy-2-methylene-3-phenylpropanenitrile. The stability of the nitrile hydratase during the repeated use of the biocatalyst was dependent on the type of the substrate. The enzyme was most stable during the transformation of (R,S)-3-hydroxy-2-methylenebutanenitrile. No significant loss of the amidase activity was observed within the course of the biocatalytic reaction Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were immobilized in lens-shaped hydrogel particles. LentiKats (R). The immobilized biocatalyst was applied to the biotransformation of benzonitrile, 3-cyanopyridine, (R,S)-3-hydroxy-2-methylenebutanenitrile and (R,S)-3-hydroxy-2-methylene-3-phenylpropanenitrile. The stability of the nitrile hydratase during the repeated use of the biocatalyst was dependent on the type of the substrate. The enzyme was most stable during the transformation of (R,S)-3-hydroxy-2-methylenebutanenitrile. No significant loss of the amidase activity was observed within the course of the biocatalytic reaction
dcterms:title
Biotransformace nitrilů pomocí baktérie Rhodococcus equi A4 imobilizované v LentiKats Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats
skos:prefLabel
Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats Biotransformation of nitriles by Rhodococcus equi A4 immobilized in LentiKats Biotransformace nitrilů pomocí baktérie Rhodococcus equi A4 imobilizované v LentiKats
skos:notation
RIV/61388971:_____/06:00039333!RIV07-GA0-61388971
n3:strany
59;61
n3:aktivita
n15:Z n15:P
n3:aktivity
P(GA203/05/2267), P(IAA4020213), P(OC D25.001), Z(AV0Z50200510)
n3:cisloPeriodika
-
n3:dodaniDat
n14:2007
n3:domaciTvurceVysledku
n16:4959175 n16:3608182
n3:druhVysledku
n18:J
n3:duvernostUdaju
n17:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
467148
n3:idVysledku
RIV/61388971:_____/06:00039333
n3:jazykVysledku
n6:eng
n3:klicovaSlova
nitrile hydratase; amidase; nitriles
n3:klicoveSlovo
n11:nitriles n11:nitrile%20hydratase n11:amidase
n3:kodStatuVydavatele
NL - Nizozemsko
n3:kontrolniKodProRIV
[3E220A3AC19D]
n3:nazevZdroje
Journal of Molecular Catalysis B-Enzymatic
n3:obor
n9:EE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
9
n3:projekt
n13:GA203%2F05%2F2267 n13:OC%20D25.001 n13:IAA4020213
n3:rokUplatneniVysledku
n14:2006
n3:svazekPeriodika
39
n3:tvurceVysledku
Martínková, Ludmila Lemaire, M. Čejková, A. Masák, J. Bolte, J. Kubáč, David Jirků, V. Stloukal, R. Gallienne, E.
n3:zamer
n10:AV0Z50200510
s:issn
1381-1177
s:numberOfPages
3