On the localization of xylanolytic enzymes in Prevotella Bryantii B14

Prevotella bryantii B14 is a strictly anaerobic, Gram-negative, polysaccharides-degrading ruminal bacterium. EDTA/sphaeroplasting and osmotic shock procedure were used in present work to localise endoxylanolytic, b -xylosidase and a -L-arabinofuranosidase activities of P. bryantii B14. Late exponen...

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Main Authors: Romana MARINŠEK-LOGAR, Franc Viktor NEKREP
Format: Article
Language:English
Published: University of Ljubljana Press (Založba Univerze v Ljubljani) 1997-12-01
Series:Acta Agriculturae Slovenica
Subjects:
Online Access:https://journals.uni-lj.si/aas/article/view/16053
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author Romana MARINŠEK-LOGAR
Franc Viktor NEKREP
author_facet Romana MARINŠEK-LOGAR
Franc Viktor NEKREP
author_sort Romana MARINŠEK-LOGAR
collection DOAJ
description Prevotella bryantii B14 is a strictly anaerobic, Gram-negative, polysaccharides-degrading ruminal bacterium. EDTA/sphaeroplasting and osmotic shock procedure were used in present work to localise endoxylanolytic, b -xylosidase and a -L-arabinofuranosidase activities of P. bryantii B14. Late exponential phase cells released most of the endoxylanolytic and CMC-ase activity by osmotic shock, showing the periplasmic location of both enzymatic activities, while b -xylosidase and a -L-arabinofuranosidase activities were recovered largely in membrane cell fraction. About 23 % of the total culture endoxylanase activity and about 30 % of the CMC-ase activity were found to be extracellular. No b -xylosidase and a -L-arabinofuranosidase activities were detected in culture supernatant of P. bryantii B14.
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issn 1854-1941
language English
publishDate 1997-12-01
publisher University of Ljubljana Press (Založba Univerze v Ljubljani)
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spelling doaj-art-6228f4b0ded947eaa1efe74c331fb0a52025-08-20T02:57:02ZengUniversity of Ljubljana Press (Založba Univerze v Ljubljani)Acta Agriculturae Slovenica1854-19411997-12-0170110.14720/aas.1997.70.1.16053On the localization of xylanolytic enzymes in Prevotella Bryantii B14Romana MARINŠEK-LOGAR0Franc Viktor NEKREP1Univ. of Ljubljana, Biotechnical Fac., Zootechnical Dept., Groblje 3, SI-1230 Domžale, SloveniaUniv. of Ljubljana, Biotechnical Fac., Zootechnical Dept., Groblje 3, SI-1230 Domžale, Slovenia Prevotella bryantii B14 is a strictly anaerobic, Gram-negative, polysaccharides-degrading ruminal bacterium. EDTA/sphaeroplasting and osmotic shock procedure were used in present work to localise endoxylanolytic, b -xylosidase and a -L-arabinofuranosidase activities of P. bryantii B14. Late exponential phase cells released most of the endoxylanolytic and CMC-ase activity by osmotic shock, showing the periplasmic location of both enzymatic activities, while b -xylosidase and a -L-arabinofuranosidase activities were recovered largely in membrane cell fraction. About 23 % of the total culture endoxylanase activity and about 30 % of the CMC-ase activity were found to be extracellular. No b -xylosidase and a -L-arabinofuranosidase activities were detected in culture supernatant of P. bryantii B14. https://journals.uni-lj.si/aas/article/view/16053rumenanaerobic bacteriaPrevotella bryantiixylanasesenzyme localization
spellingShingle Romana MARINŠEK-LOGAR
Franc Viktor NEKREP
On the localization of xylanolytic enzymes in Prevotella Bryantii B14
Acta Agriculturae Slovenica
rumen
anaerobic bacteria
Prevotella bryantii
xylanases
enzyme localization
title On the localization of xylanolytic enzymes in Prevotella Bryantii B14
title_full On the localization of xylanolytic enzymes in Prevotella Bryantii B14
title_fullStr On the localization of xylanolytic enzymes in Prevotella Bryantii B14
title_full_unstemmed On the localization of xylanolytic enzymes in Prevotella Bryantii B14
title_short On the localization of xylanolytic enzymes in Prevotella Bryantii B14
title_sort on the localization of xylanolytic enzymes in prevotella bryantii b14
topic rumen
anaerobic bacteria
Prevotella bryantii
xylanases
enzyme localization
url https://journals.uni-lj.si/aas/article/view/16053
work_keys_str_mv AT romanamarinseklogar onthelocalizationofxylanolyticenzymesinprevotellabryantiib14
AT francviktornekrep onthelocalizationofxylanolyticenzymesinprevotellabryantiib14