Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/2636

TitleImmobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
Author(s)Costa, Silgia
Tzanov, Tzanko
Paar, Andreas
Gudelj, Marinka
Gübitz, Georg M.
Paulo, Artur Cavaco
KeywordsCatalase
Covalent immobilization
Thermo- and alkaline stability
Hydrogen peroxide
Issue date2001
PublisherElsevier
JournalEnzyme and Microbial Technology
Citation"Enzyme and Microbial Technology". ISSN 0141-0229. 28:9-10 (June 2001) 815–819.
Abstract(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.
TypeArticle
URIhttp://hdl.handle.net/1822/2636
DOI10.1016/S0141-0229(01)00335-0
ISSN0141-0229
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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