About: Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots     Goto   Sponge   NotDistinct   Permalink

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  • The main form of pectate hydrolases in the cell wall of parsley roots showed a unique substrate preference of a plant exopolygalacturonase because it clearly preferred the substrates with degree of polymerization about 10. This form was separated from the others, purified and characterized. Enzyme exhibited sharp pH optimum corresponding to pH 4.7, molecular mass 53.5 kDa, and isoelectric point 5.3. It was stable at 50A degrees C in 2-h assay and had optimum of temperature at 60A degrees C (activation energy being 37.0 kJ/mol). The interaction with concanavalin A indicated the glycosylation of enzyme. Substrates were cleaved from the non-reducing end.
  • The main form of pectate hydrolases in the cell wall of parsley roots showed a unique substrate preference of a plant exopolygalacturonase because it clearly preferred the substrates with degree of polymerization about 10. This form was separated from the others, purified and characterized. Enzyme exhibited sharp pH optimum corresponding to pH 4.7, molecular mass 53.5 kDa, and isoelectric point 5.3. It was stable at 50A degrees C in 2-h assay and had optimum of temperature at 60A degrees C (activation energy being 37.0 kJ/mol). The interaction with concanavalin A indicated the glycosylation of enzyme. Substrates were cleaved from the non-reducing end. (en)
Title
  • Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
  • Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots (en)
skos:prefLabel
  • Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
  • Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots (en)
skos:notation
  • RIV/00216305:26310/09:PU86526!RIV12-MSM-26310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(AV0Z40310501), Z(MSM0021630501)
http://linked.open...iv/cisloPeriodika
  • 2
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
  • 331273
http://linked.open...ai/riv/idVysledku
  • RIV/00216305:26310/09:PU86526
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • EXO-D-GALACTURONANASE, ASPERGILLUS-NIGER, GLYCOSIDE HYDROLASES, BIOCHEMICAL-CHARACTERIZATION, ENDOPOLYGALACTURONASE-I, CRYSTAL-STRUCTURE, EXOPOLYGALACTURONASE, POLYGALACTURONASE, CARROT, CHROMATOGRAPHY (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CZ - Česká republika
http://linked.open...ontrolniKodProRIV
  • [F44FE931F9EC]
http://linked.open...i/riv/nazevZdroje
  • Biológia
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 2009 (64)
http://linked.open...iv/tvurceVysledku
  • Flodrová, Dana
  • Omelková, Jiřina
  • Stratilová, Eva
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-3088
number of pages
http://localhost/t...ganizacniJednotka
  • 26310
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