Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/2393
Registo completo
Campo DC | Valor | Idioma |
---|---|---|
dc.contributor.author | Costa, Silgia | - |
dc.contributor.author | Tzanov, Tzanko | - |
dc.contributor.author | Carneiro, Ana Filipa Gonçalves da Costa | - |
dc.contributor.author | Paar, Andreas | - |
dc.contributor.author | Gübitz, Georg M. | - |
dc.contributor.author | Paulo, Artur Cavaco | - |
dc.date.accessioned | 2005-07-08T11:21:59Z | - |
dc.date.available | 2005-07-08T11:21:59Z | - |
dc.date.issued | 2002-03 | - |
dc.identifier.citation | "Enzyme and microbial technology". ISSN 0141-0229. 30:3 (Mar. 2002) 387–391. | eng |
dc.identifier.issn | 0141-0229 | - |
dc.identifier.uri | https://hdl.handle.net/1822/2393 | - |
dc.description.abstract | Native catalase preparations isolated from Bacillus Sp were formulated with different additives for storage stabilization and better performance at high temperature and pH. The additives studied were: polyethylene glycol, glycerol, BSA, casein, glutaraldehyde, n-butylamine, ethylenediamine, 1.6-diaminohexane, BSA/glutaraldehyde and casein/glutaraldehyde. The glycerol and glutaraldehyde showed the best performance for long-term storage at 30degreesC and neutral pH. No stabilization additives were effective at pH 12, but below that pH the polyethylene glycol and glycerol appeared to be the most appropriate. Amines, polyethylene glycol and glycerol shifted the pH activity maximum of the native catalase toward more alkaline region, while glycerol were the only additive to improve the temperature profile of the enzyme. (C) 2002 Elsevier Science Inc. All rights reserved. | por |
dc.language.iso | eng | eng |
dc.publisher | Elsevier 1 | eng |
dc.rights | openAccess | eng |
dc.subject | hydrogen peroxide | por |
dc.subject | catalase | por |
dc.subject | thermo and alkaline stability | por |
dc.subject | additives | por |
dc.title | Studies of stabilization of native catalase using additives | eng |
dc.type | article | eng |
dc.peerreviewed | yes | eng |
oaire.citationStartPage | 387 | por |
oaire.citationEndPage | 391 | por |
oaire.citationIssue | 3 | por |
oaire.citationVolume | 30 | por |
dc.identifier.doi | 10.1016/S0141-0229(01)00505-1 | por |
dc.subject.wos | Science & Technology | por |
sdum.journal | Enzyme and Microbial Technology | por |
Aparece nas coleções: | DET/2C2T - Artigos em revistas internacionais com arbitragem científica |