About: Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose     Goto   Sponge   NotDistinct   Permalink

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Description
  • Pyranose dehydrogenase of the mushroom Agaricus meleagris was purified from mycelial culture media using ion-exchange and hydrophobic interaction chromatography. The native enzyme is a monomeric polypeptide with a molecular mass of 66,547 Da, containing 7% carbohydrate and covalently bound flavin adenine dinucleotide. The enzyme oxidized different aldopyranoses to the corresponding C-2 or C-2,3 (di)dehydro sugars. Preferred electron donors with the highest kcat/Km values were major sugar constituents of cellulose and hemicellulose, namely D-glucose, D-galactose, L-arabinose, D-xylose and cellobiose
  • Pyranose dehydrogenase of the mushroom Agaricus meleagris was purified from mycelial culture media using ion-exchange and hydrophobic interaction chromatography. The native enzyme is a monomeric polypeptide with a molecular mass of 66,547 Da, containing 7% carbohydrate and covalently bound flavin adenine dinucleotide. The enzyme oxidized different aldopyranoses to the corresponding C-2 or C-2,3 (di)dehydro sugars. Preferred electron donors with the highest kcat/Km values were major sugar constituents of cellulose and hemicellulose, namely D-glucose, D-galactose, L-arabinose, D-xylose and cellobiose (en)
  • Pyranosadehydrogenasa Agaricus meleagris byla purifikována z media myceliálních kultur této houby užitím ionexové a hydrofobně-interakční chromatografie. Nativní enzym byl charakterizován jako monomerní polypeptid o molekulární hmotnosti 66 547 Da, obsahující 7% sacharidu a kovalentně vázaný flavinadenindinukleotid. Oxidoval různé aldopyranosy na odpovídající C-2 či C-2,3 (di)dehydrocukry (cs)
Title
  • Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose
  • Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose (en)
  • Charakterizace pyranosadehydrogenasy z Agaricus meleagris a její využití k C-2 specifické konversi D-galaktosy (cs)
skos:prefLabel
  • Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose
  • Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose (en)
  • Charakterizace pyranosadehydrogenasy z Agaricus meleagris a její využití k C-2 specifické konversi D-galaktosy (cs)
skos:notation
  • RIV/61388971:_____/08:00313090!RIV09-AV0-61388971
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika
  • 3
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 359611
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/08:00313090
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • pyranose dehydrogenase; sugar oxidoreductase; galactose coversion (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [BFA068A40220]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biotechnology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 133
http://linked.open...iv/tvurceVysledku
  • Halada, Petr
  • Haltrich, D.
  • Volc, Jindřich
  • Peterbauer, C.
  • Kubátová, Elena
  • Sygmund, Ch.
  • Kittl, R.
http://linked.open...ain/vavai/riv/wos
  • 000252632200009
http://linked.open...n/vavai/riv/zamer
issn
  • 0168-1656
number of pages
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