Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Sheila I. McCrae"'
Publikováno v:
FEMS Microbiology Ecology. 66:487-495
β-Glycosidase activities present in the human colonic microbiota act on glycosidic plant secondary compounds and xenobiotics entering the colon, with potential health implications for the human host. Information on β-glycosidases is currently limit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b46c374dbbe67a3202c55aa95cb7efd
https://doi.org/10.1111/j.1574-6941.2008.00520.x
https://doi.org/10.1111/j.1574-6941.2008.00520.x
Publikováno v:
FEMS Microbiology Letters. 269:240-247
Butyrate producers constitute an important bacterial group in the human large intestine. Butyryl-CoA is formed from two molecules of acetyl-CoA in a process resembling β-oxidation in reverse. Three different arrangements of the six genes coding for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::75e13676e49d22ec68dfb9195f82ac4d
https://doi.org/10.1111/j.1574-6968.2006.00629.x
https://doi.org/10.1111/j.1574-6968.2006.00629.x
Autor:
Michelle S. Jackson, Harry J. Flint, Jacqueline Millar, Sylvia H. Duncan, Petra Louis, Sheila I. McCrae
Publikováno v:
Journal of Bacteriology. 186:2099-2106
The final steps in butyrate synthesis by anaerobic bacteria can occur via butyrate kinase and phosphotransbutyrylase or via butyryl-coenzyme A (CoA):acetate CoA-transferase. Degenerate PCR and enzymatic assays were used to assess the presence of buty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe3ec3ff029d0b5504a819caeb2272d8
https://doi.org/10.1128/jb.186.7.2099-2106.2004
https://doi.org/10.1128/jb.186.7.2099-2106.2004
Publikováno v:
Applied and Environmental Microbiology. 67:4426-4431
The mechanisms by which cellulolytic enzymes and enzyme complexes in Ruminococcus spp. bind to cellulose are not fully understood. The product of the newly isolated cellulase gene endB from Ruminococcus flavefaciens 17 was purified as a His-tagged pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cca7bd7bfff7996633a530ecaa798c78
https://doi.org/10.1128/aem.67.10.4426-4431.2001
https://doi.org/10.1128/aem.67.10.4426-4431.2001
Autor:
Jennifer C. Martin, Sheila I. McCrae, Harry J. Flint, Marco T. Rincon, Vincenzo Aurilia, Karen P. Scott
Publikováno v:
Microbiology. 146:1391-1397
Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17. The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cbe74e5441404346b720f9f23e0bdec
https://doi.org/10.1099/00221287-146-6-1391
https://doi.org/10.1099/00221287-146-6-1391
Publikováno v:
Journal of Biotechnology. 43:183-194
A number of fungi were screened for their capacities to produce extracellular α-(4-O-methyl)- d -glucuronidase. Of those tested, Phanerochaete chrysosporium ATCC 24725 produced the enzyme in greatest yield. The single α-(4-O-methyl)- d -glucuronida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9cdf2afed3a040cef3509c20565d08c
https://doi.org/10.1016/0168-1656(95)00128-x
https://doi.org/10.1016/0168-1656(95)00128-x
Publikováno v:
Applied Microbiology and Biotechnology. 44:177-184
Seven fractions rich in endoglucanase activity were separated from the extracellular cellulase system of the anaerobic rumen fungus Neocallimastix frontalis. The fractions (ES1, ES3, ES2U1, ES2U2, ES2U4, ES2U3C1 and ES2U3C2) were separated from each
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b004525f9c4de3b97a95d44817a18525
https://doi.org/10.1007/bf00164499
https://doi.org/10.1007/bf00164499
Publikováno v:
Journal of Biotechnology. 37:217-227
A β- d -glucosidase was purified by a series of chromatographic procedures involving gel filtration, ion exchange, adsorption/desorption on hydroxyapatite and hydrophobic interaction. The enzyme had an isoelectric pH of 3.7 and an apparent molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0dd8e985a083418dba9b4b6fc7493dd9
https://doi.org/10.1016/0168-1656(94)90129-5
https://doi.org/10.1016/0168-1656(94)90129-5
Publikováno v:
Enzyme and Microbial Technology. 16:826-834
Feruloyl esterase and p -coumaroyl esterase activities were separated by ion-exchange chromatography on a column of DEAE-Sepharose CL 6B and then purified by hydrophobic interaction chromatography and anion-exchange chromatography, respectively. Feru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d26fee6410e13290598f1e2343a1fdd7
https://doi.org/10.1016/0141-0229(94)90055-8
https://doi.org/10.1016/0141-0229(94)90055-8
Publikováno v:
Enzyme and Microbial Technology. 14:875-884
A purified extracellular phenolic acid esterase, produced by the fungus Penicillium pinophilum in solid-state culture, released ferulic and ϱ-coumaric acid from methyl esters of the acids. The esterase was also able to release all the alkali-extract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::75dde3931162441fb643907269227110
https://doi.org/10.1016/0141-0229(92)90050-x
https://doi.org/10.1016/0141-0229(92)90050-x