Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/2636| Título: | Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents |
| Autor(es): | Costa, Silgia Tzanov, Tzanko Paar, Andreas Gudelj, Marinka Gübitz, Georg M. Paulo, Artur Cavaco |
| Palavras-chave: | Catalase Covalent immobilization Thermo- and alkaline stability Hydrogen peroxide |
| Data: | 2001 |
| Editora: | Elsevier 1 |
| Revista: | Enzyme and Microbial Technology |
| Citação: | "Enzyme and Microbial Technology". ISSN 0141-0229. 28:9-10 (June 2001) 815–819. |
| Resumo(s): | A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as
crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and
immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the
immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11,
30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants
added to the hydrogen peroxide substrate solution. A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11, 30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants added to the hydrogen peroxide substrate solution. |
| Tipo: | Artigo |
| URI: | https://hdl.handle.net/1822/2636 |
| DOI: | 10.1016/S0141-0229(01)00335-0 |
| ISSN: | 0141-0229 |
| Arbitragem científica: | yes |
| Acesso: | Acesso aberto |
| Aparece nas coleções: | DET/2C2T - Artigos em revistas internacionais com arbitragem científica |
