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Description
  • Chitinolytický systém anaerobních polycentrických bachorových hub rodu Orpinomyces a Anaeromyces byl studován ve třech frakcích- extracelulární, cytosolické frakce a frakce z buněčných stěn. Endochitinasa představovala dominantní enzym s nejvyšší aktivitou v cytosolické frakci. Endochitinasa u obou rodů byla stabilní v rozmezí pH 4,5 až 7 s optimálním pH 6,5. Endochitinasa u Orpinomyces byla stabilní do 50°C s optimální teplotou 50°C. Endochitinasa z Anaeromyces byla stabilní do 40°C s optimální teplotou 40°C. Nejvhodnějším substrátem pro endochitinasu u obou rodů byl chitin izolovaný z houbových buněčných stěn. Enzymová aktivita obou endochitinas byla inhibována iontem Hg2+ a aktivována iontem Mg2+. Obě endochitinasy byli inhibovány 10 mM SDS a aktivovány iodoacetamidem. (cs)
  • Chitinolytic system of anaerobic polycentric rumen fungi of genera Orpinomyces and Anaeromyces was studied in three crude enzyme fractions- extracellular, cytosolic and cell wall fraction. Endochitinase was found as a dominant enzyme with highest activity in cytosolic fraction. Endochitinases of both genera were stable from pH 4.5 to 7 with optimal pH 6.5. Orpinomyces endochitinase was stable up to 50 0C with optimal temperature 50 0C. Anaeromyces endochitinase was stable up to 40 0C with optimal temperature also 40 0C. The most suitable substrate for both endochitinases was fungal cell wall chitin. Enzyme activities were inhibited by Hg2+ ions and activated by Mg2+ ions. Both endochitinases were inhibited by 10 mM SDS and activated by iodacetamide.
  • Chitinolytic system of anaerobic polycentric rumen fungi of genera Orpinomyces and Anaeromyces was studied in three crude enzyme fractions- extracellular, cytosolic and cell wall fraction. Endochitinase was found as a dominant enzyme with highest activity in cytosolic fraction. Endochitinases of both genera were stable from pH 4.5 to 7 with optimal pH 6.5. Orpinomyces endochitinase was stable up to 50 0C with optimal temperature 50 0C. Anaeromyces endochitinase was stable up to 40 0C with optimal temperature also 40 0C. The most suitable substrate for both endochitinases was fungal cell wall chitin. Enzyme activities were inhibited by Hg2+ ions and activated by Mg2+ ions. Both endochitinases were inhibited by 10 mM SDS and activated by iodacetamide. (en)
Title
  • Characterization of chitinases of polycentric anaerobic rumen fungi
  • Characterization of chitinases of polycentric anaerobic rumen fungi (en)
  • Charakterizace chitinas polycentrických anaerobních bachorových hub (cs)
skos:prefLabel
  • Characterization of chitinases of polycentric anaerobic rumen fungi
  • Characterization of chitinases of polycentric anaerobic rumen fungi (en)
  • Charakterizace chitinas polycentrických anaerobních bachorových hub (cs)
skos:notation
  • RIV/67985904:_____/08:00312643!RIV09-AV0-67985904
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(AV0Z50450515)
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
  • 359578
http://linked.open...ai/riv/idVysledku
  • RIV/67985904:_____/08:00312643
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • endochitinase; anaerobic; rumen fungi (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CZ - Česká republika
http://linked.open...ontrolniKodProRIV
  • [1C286AB424B3]
http://linked.open...i/riv/nazevZdroje
  • Folia Microbiologica
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 53
http://linked.open...iv/tvurceVysledku
  • Fliegerová, Kateřina
  • Šimůnek, Jiří
  • Novotná, Zuzana
http://linked.open...ain/vavai/riv/wos
  • 000257941200014
http://linked.open...n/vavai/riv/zamer
issn
  • 0015-5632
number of pages
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