Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Geobacillus pallidus"'
Publikováno v:
Acta Chimica Slovaca. 7:57-63
A bacterial strain was isolated from Pasinler hot spring, Erzurum, Turkey. The purified thermophilic isolate was identified as Geobacillus pallidus P26 and used to produce extracellular pectin lyase (EC 4.2.2.10). Pectin lyase enzyme was purified 34
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3d9f3d7855fc1da9418fb7b080800f0
https://doi.org/10.2478/acs-2014-0011
https://doi.org/10.2478/acs-2014-0011
Autor:
EFSA Panel on Biological Hazards (BIOHAZ), Allende, Ana, Bolton, Declan, Chemaly, Marianne, Davies, Robert, Fernandez Escamez, Pablo Salvador, Girones, Rosina, Herman, Lieve, Koutsoumanis, Konstantinos, Lindqvist, Roland, Nørrung, Birgit, Ricci, Antonia, Robertson, Lucy, Ru, Giuseppe, Sanaa, Moez, Simmons, Marion, Skandamis, Panagiotis, Snary, Emma, Speybroeck, Niko, Ter Kuile, Benno, Threlfall, John, Wahlström, Helene
Publikováno v:
EFSA Journal, Vol. 14, no.7, p. 4522 [1-37] (2016)
EFSA Journal, Vol 14, Iss 7, Pp n/a-n/a (2016)
EFSA Journal, Vol 14, Iss 7, Pp n/a-n/a (2016)
EFSA was requested to assess the safety of a broad range of biological agents in the context of notifications for market authorisation as sources of food and feed additives, enzymes and plant protection products. The qualified presumption of safety (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d013fd4af0be0e677c02ec4647c2f6ec
https://hdl.handle.net/2078.1/188331
https://hdl.handle.net/2078.1/188331
Autor:
Mavengere, William Nyasha
Magister Scientiae - MSc
Nitrile hydratases (NHases) are enzymes that catalyse the conversion of organocyanides to amides via a non-hydrolytic hydration reaction. They are industrially relevant enzymes, currently used in the manufacture of nicot
Nitrile hydratases (NHases) are enzymes that catalyse the conversion of organocyanides to amides via a non-hydrolytic hydration reaction. They are industrially relevant enzymes, currently used in the manufacture of nicot
Externí odkaz:
http://hdl.handle.net/11394/2786
Autor:
Williamson, D S, Dent, K C, Weber, B W, Varsani, A, Frederick, J, Thuku, R, Cameron, R A, van Heerden, J H, Cowan, D A, Sewell, B T
Publikováno v:
Applied Microbiology and Biotechnology
Geobacillus pallidus RAPc8 (NRRL: B-59396) is a moderately thermophilic gram-positive bacterium, originally isolated from Australian lake sediment. The G. pallidus RAPc8 gene encoding an inducible nitrilase was located and cloned using degenerate pri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3158::6ba219f8b89c42ac2a28d2e5ccbd82a8
http://hdl.handle.net/11427/20737
http://hdl.handle.net/11427/20737
Autor:
Mavengere, William Nyasha.
Nitrile hydratases (NHases) are enzymes that catalyse the conversion of organocyanides to amides via a non-hydrolytic hydration reaction. They are industrially relevant enzymes, currently used in the manufacture of nicotinamide and acrylamide. The ta
Externí odkaz:
http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_4827_1271013260
Publikováno v:
Acta Crystallographica. Section D, Biological Crystallography
The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase superfamily and catalyzes the conversion of amides to the corresponding carboxylic acids and ammonia. It shows both amide-hydrolysis and acyl-transfer a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::266a15bffc8755605952e6f26989ac0c
https://hdl.handle.net/11427/21005
https://hdl.handle.net/11427/21005
Publikováno v:
Acta crystallographica Section F, Structural biology and crystallization communications
The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase enzyme superfamily. It converts amides to the corresponding acids and ammonia and has application as an industrial catalyst. RAPc8 amidase has been clon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3158::725421bc21a51db0579ddb97404a62e2
http://hdl.handle.net/11427/21637
http://hdl.handle.net/11427/21637
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