Zobrazeno 1 - 10
of 20
pro vyhledávání: '"T. Čepeljnik"'
Publikováno v:
Folia Microbiologica. 52:367-373
Pseudobutyrivibrio xylanivorans strain Mz5(T), an anaerobic bacterium (originating from the rumen of a Holstein-Friesian cow), has some attributes that make it a possible probiotic strain (very active hydrolases, bacteriocin and conjugated linoleic a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb00c9bdf2f44fca50ef5334bdc12d01
https://doi.org/10.1007/bf02932091
https://doi.org/10.1007/bf02932091
Autor:
T. Čepeljnik, Yoav Barak, Harry J. Flint, Jennifer C. Martin, Edward A. Bayer, Marco T. Rincon, Raphael Lamed
Publikováno v:
Journal of Bacteriology. 189:4774-4783
Ruminococcus flavefaciens produces a cellulosomal enzyme complex, based on the structural proteins ScaA, -B, and -C, that was recently shown to attach to the bacterial cell surface via the wall-anchored protein ScaE. ScaA, -B, -C, and -E are all cohe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c799a585a31af947551212afe43874f
https://doi.org/10.1128/jb.00143-07
https://doi.org/10.1128/jb.00143-07
Publikováno v:
Folia Microbiologica. 51:263-267
The rumen bacterium Pseudobutyrivibrio xylanivorans Mz5T has a potent xylanolytic enzyme system. A small native peptide (approximately 30-kDa, designated Xyn11A) from the bacterium was first isolated and characterized by Edman degradation. The gene c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efd441df580157d100f8a58144c884a4
https://doi.org/10.1007/bf02931809
https://doi.org/10.1007/bf02931809
Autor:
Yoav Barak, Marco T. Rincon, Harry J. Flint, Edward A. Bayer, T. Čepeljnik, Jennifer C. Martin, Raphael Lamed
Publikováno v:
Journal of Bacteriology. 187:7569-7578
Sequence extension of the scaffoldin gene cluster from Ruminococcus flavefaciens revealed a new gene ( scaE ) that encodes a protein with an N-terminal cohesin domain and a C terminus with a typical gram-positive anchoring signal for sortase-mediated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db59cc751246aeabbd0c160aad8b4ace
https://doi.org/10.1128/jb.187.22.7569-7578.2005
https://doi.org/10.1128/jb.187.22.7569-7578.2005
Publikováno v:
Enzyme and Microbial Technology. 34:219-227
Rumen bacterium Pseudobutyrivibrio xylanivorans Mz5T produces multiple xylanases that account for its high xylanolytic activity. The smallest xylanase (XynT) accounts for the majority of the activity in the later growth phases. This enzyme was purifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b9fa17b8b1105eb2c194b36fbc49718
https://doi.org/10.1016/j.enzmictec.2003.10.012
https://doi.org/10.1016/j.enzmictec.2003.10.012
Publikováno v:
Folia Microbiologica. 48:339-345
Rumen bacterium Pseudobutyrivibrio xylanivorans strain Mz5T possessed a potent xylanolytic enzyme system consisting of at least 7 different xylan hydrolases with molar mass 27-145 kDa. Three of them were successfully isolated in active native form. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edf8835db04b7be844372f0228f68e2b
https://doi.org/10.1007/bf02931363
https://doi.org/10.1007/bf02931363
Publikováno v:
Environmental monitoring and assessment. 139(1-3)
Combining genotoxicity/mutagenicity tests and physico-chemical methodologies can be useful for determining the potential genotoxic contaminants in soil samples. The aim of our study was to evaluate the genotoxicity of soil by applying an integrated p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bed2e094d231bf5717b6c56f84ab4da
https://pubmed.ncbi.nlm.nih.gov/17566864
https://pubmed.ncbi.nlm.nih.gov/17566864
Publikováno v:
Folia microbiologica. 46(1)
Butyrivibrio sp. Mz 5 with a high xylanolytic activity was isolated. Four major xylanases were detected in the cell-associated fraction using the zymogram technique. The xylanolytic activity was inducible with the oat spelts xylan; two endoxylanases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80723a497daf3414aa97412d1f559267
https://pubmed.ncbi.nlm.nih.gov/11501489
https://pubmed.ncbi.nlm.nih.gov/11501489
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