Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Rahman Rahmanpour"'
Autor:
Rahman Rahmanpour, Timothy D. H. Bugg, María Jesús Durán-Peña, Devin James Sapsford, Goran M. M. Rashid
Publikováno v:
Journal of Applied Microbiology. 123:159-171
Aims\ud \ud The aim of the study was to isolate bacterial lignin-degrading bacteria from municipal solid waste soil, and to investigate whether they could be used to delignify lignocellulose-containing soil, and enhance methane release.\ud Methods an
Publikováno v:
Biotechnology and Applied Biochemistry. 64:803-809
An extracellular esterase gene estK was identified in Pseudomonas putida mt-2 and overexpressed at high levels in Escherichia coli. The recombinant EstK enzyme was purified and characterized kinetically against p-nitrophenyl ester and other aryl-alky
Autor:
Timothy D. H. Bugg, Rahman Rahmanpour
Publikováno v:
Archives of Biochemistry and Biophysics. 574:93-98
Members of the DyP family of peroxidases in Gram-positive bacteria have recently been shown to oxidise Mn(II) and lignin model compounds. Gram-negative pseudomonads, which also show activity for lignin oxidation, also contain dyp-type peroxidase gene
A significant problem in the oxidative breakdown of lignin is the tendency of phenolic radical fragments to re-polymerise to form higher molecular weight species. In this paper we identify an extracellular flavin-dependent dehydrolipoamide dehydrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cec2e414a787923b0b19d70688e42d9
Autor:
Robert, Millar, Rahman, Rahmanpour, Eugenie Wei Jia, Yuan, Catharine, White, Timothy D H, Bugg
Publikováno v:
Biotechnology and applied biochemistry. 64(6)
An extracellular esterase gene estK was identified in Pseudomonas putida mt-2 and overexpressed at high levels in Escherichia coli. The recombinant EstK enzyme was purified and characterized kinetically against p-nitrophenyl ester and other aryl-alky
A Dyp-type peroxidase enzyme from thermophilic cellulose degrader Thermobifida fusca (TfuDyP) was investigated for catalytic ability towards lignin oxidation. TfuDyP was characterised kinetically against a range of phenolic substrates, and a compound
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65c7454ee84553d5f4955ec8467ce1cd
http://wrap.warwick.ac.uk/77595/1/WRAP_Bugg_Structure.pdf
http://wrap.warwick.ac.uk/77595/1/WRAP_Bugg_Structure.pdf
Publikováno v:
Production of Biofuels and Chemicals from Lignin ISBN: 9789811019647
Although microbial lignin degradation has been studied mainly in fungi, in recent years several bacterial enzymes capable of lignin oxidation have been discovered. Pathway engineering studies in genetically tractable bacterial lignin degraders have s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afac58a83686deb0592b0bf1dd2eb410
https://doi.org/10.1007/978-981-10-1965-4_5
https://doi.org/10.1007/978-981-10-1965-4_5
Autor:
Timothy D. H. Bugg, Rahman Rahmanpour
Publikováno v:
Heme Peroxidases ISBN: 9781849739115
The dye-decolorizing peroxidases are a recently discovered family of bacterial and fungal peroxidases that are structurally unrelated to the previously studied mammalian and plant peroxidases, but show novel reactivity for oxidation of anthraquinone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::314cd8405b3b56be62fa178ba830d20c
https://doi.org/10.1039/9781782622628-00334
https://doi.org/10.1039/9781782622628-00334
Autor:
Timothy D. H. Bugg, Rahman Rahmanpour
Publikováno v:
Current opinion in chemical biology. 29
The aromatic heteropolymer lignin is a major component of plant cell walls, and is produced industrially from paper/pulp manufacture and cellulosic bioethanol production. Conversion of lignin into renewable chemicals is a major unsolved problem in th
Autor:
Rahman Rahmanpour, Timothy D. H. Bugg
Rhodococcus jostii RHA1 peroxidase DypB has been recently identified as a bacterial lignin peroxidase. The dypB gene is cotranscribed with a gene encoding an encapsulin protein, which has been shown in Thermotoga maritima to assemble to form a 60-sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6f407d232a11a5e708be2141376ffd4