Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Maria Wojciechowicz"'
Autor:
Maria Wojciechowicz
Publikováno v:
Toruńskie Studia Bibliologiczne, Vol 6, Iss 1 (10), Pp 23-40 (2013)
The article presents the history of music industry in Poland after the Second World War, in the period 1945–1955, on political background. The “Muza” music company, a well-known label in Poland in the era of socialism, was described. The organi
Externí odkaz:
https://doaj.org/article/9c5e1b79f8154f0e894556a08e558bec
Drought stress inducing pollen sterility can reduce crop yield worldwide. The regulatory crosstalk associated with the effects of drought on pollen formation at the cellular level have not been explored in detail so far. In this study, we performed m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35fbba70807aecabe0e54d9afa2139f0
https://doi.org/10.20944/preprints202304.0371.v1
https://doi.org/10.20944/preprints202304.0371.v1
Publikováno v:
Letters in Applied Microbiology. 15:244-247
Degradation of fructan obtained from timothy (Phleum pratense L.) by the following six species of bacteria isolated from sheep rumen was studied: Streptococcus bovis, Bacteroides ruminicola, Selenomonas ruminantium, Butyrivibrio fibrisolvens, Trepone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa84382c302af669280f9aa994379911
https://doi.org/10.1111/j.1472-765x.1992.tb00774.x
https://doi.org/10.1111/j.1472-765x.1992.tb00774.x
Publikováno v:
Journal of Applied Bacteriology. 66:169-174
A cell-bound pectinolytic enzyme was isolated from cells of Selenomonas ruminantium and purified about 360-fold. The optimum pH and temperature for enzyme activity was 7.0 and 40 degrees C. The enzyme degraded polymeric substrates by hydrolysis of di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da4c1a3acea9194b3c98a39d67218641
https://doi.org/10.1111/j.1365-2672.1989.tb02466.x
https://doi.org/10.1111/j.1365-2672.1989.tb02466.x
Autor:
Maria Wojciechowicz, A. Ziolecki
Publikováno v:
Journal of Applied Bacteriology. 56:515-518
Wojciechowicz, M. & Ziolecki, A. 1984. A note on the pectinolytic enzyme of Streptococcus bovis. Journal of Applied Bacteriology56, 515–518. A pectinolytic strain of Streptococcus bovis isolated from the bovine rumen produced an endopolygalacturona
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38ba6339b471484fda81dbb923329e5f
https://doi.org/10.1111/j.1365-2672.1984.tb01383.x
https://doi.org/10.1111/j.1365-2672.1984.tb01383.x
Autor:
Maria Wojciechowicz, A. Ziolecki
Publikováno v:
Archiv für Tierernaehrung. 15:417-427
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf60071dc29713263fe7ae15c9b50ce5
https://doi.org/10.1080/17450396509436654
https://doi.org/10.1080/17450396509436654
Publikováno v:
Letters in Applied Microbiology. 8:105-107
d-Galacturonandigalacturonohydrolase was immobilized by covalent coupling on to a polyacrylamide-type carrier BIO Gel CM100, activated by water-soluble carbodiimide. Catalytic properties, stability and action pattern of the immobilized enzyme are rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::891a7dbe352b365aaf118a674193ab29
https://doi.org/10.1111/j.1472-765x.1989.tb00234.x
https://doi.org/10.1111/j.1472-765x.1989.tb00234.x
Publikováno v:
Journal of general microbiology. 117(1)
A poly(1,4-alpha-D-galacturonide) lyase (EC 4.2.2.2) from the culture fluid of Lachnospira multiparus was purified about 20-fold. The optimum pH and temperature for enzyme activity were 8.0 and 40 degrees C. The enzyme required Ca2+ and was inhibited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4541fb7b7fadad83739a5bd8679c7ff6
https://pubmed.ncbi.nlm.nih.gov/7391818
https://pubmed.ncbi.nlm.nih.gov/7391818
Publikováno v:
Journal of general microbiology. 131(8)
Summary: An intracellular pectinolytic enzyme was isolated from a cell extract of Butyrivibrio fibrisolvens and purified. The optimum pH for enzyme activity was 5·6. The enzyme preferentially degraded de-esterified substrates by hydrolysis of monosa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a62d508cee542d7f33bcc8b3c66dea5
https://pubmed.ncbi.nlm.nih.gov/4056742
https://pubmed.ncbi.nlm.nih.gov/4056742
Autor:
A. Ziołecki, Maria Wojciechowicz
Publikováno v:
Archiv für Tierernährung Band 15, Heft 1–6 ISBN: 9783112477328
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac3bce1d8aa66701eb6066b019bcdc8d
https://doi.org/10.1515/9783112477328-035
https://doi.org/10.1515/9783112477328-035