期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 74, 期 3-4, 页码 178-183出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2011.10.002
关键词
Enzyme immobilization; Polyphosphazenes; Oxidoreductases; Baeyer-Villiger monooxygenases; Cofactor recycling
资金
- Principado de Asturias
- Spanish Ministerio de Ciencia e Innovacion (MICINN) [CTQ2007-61126, CTQ2010-18330]
- European Social Fund
- Ramon y Cajal Program
A novel method has been employed for the selective covalent co-immobilization of a Baeyer-Villiger monooxygenase (phenylacetone monooxygenase from Thermobifida fusca) and a NADPH recycling enzyme (glucose-6-phosphate dehydrogenase) on the same polyphosphazene carrier for the first time starting from {NP[O2C12H8-x(NH2)(x)]}(n) (x ranging from 0.5 to 2) using glutaraldehyde as connector. In all cases the preparation was active and it was found that the optimum proportion of amino groups in the starting polyphosphazene was 0.5 per monomer. The immobilized biocatalysts showed similar selectivity when compared with the isolated monooxygenase, demonstrating the potential of this novel type of immobilizing material, although their recyclability must still be improved. (C) 2011 Elsevier B.V. All rights reserved.
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