| Literature DB >> 11690697 |
Tzanko Tzanov1, Silgia A Costa, Georg M Gübitz, Artur Cavaco-Paulo.
Abstract
Glucose oxidase was covalently immobilized on commercially available alumina and glass supports, with a high level of protein recovery. The operational stability of the alumina carrier was an advantage over the glass support, though the rate of generation of hydrogen peroxide in the case of the latter was higher. The immobilization technique provided repeated application of the enzyme even in low concentration, and the hydrogen peroxide generated in the enzymatic reaction was successively used for textile bleaching.Entities:
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Year: 2002 PMID: 11690697 DOI: 10.1016/s0168-1656(01)00386-8
Source DB: PubMed Journal: J Biotechnol ISSN: 0168-1656 Impact factor: 3.307