期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 55, 期 3-4, 页码 177-184出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2008.03.011
关键词
Laccase; Phenol; Chemical modification; Biocatalytic membranes; Non-isothermal bioreactors
资金
- University Prof. Dr. A. Zlatarov Burgas, Bulgaria
- Italian Interuniversity Consortium National Institute for Biostructures and Biosystems (INBB)
Laccase from Rhus vernicifera was immobilized on a polypropylene membrane chemically modified with chromic acid. Ethylenediamine and glutaraldehyde were used as spacer and bifunctional coupling agent, respectively. Phenol was used as substrate. To know how the immobilization procedures affected the enzyme reaction rate the catalytic behavior Of Soluble and insoluble laccase Was Studied under isothermal conditions as a function of pH, temperature and substrate concentration. From these studies, two main Singularities emerged: (i) the narrower pH-activity profile of the Soluble enzyme in comparison to that of the insoluble counterpart and (ii) the increase in pH and thermal stability of the insoluble enzyme. The laccase catalytic behavior was also studied in a non-isothermal bioreactor as a function of substrate concentration and size of the applied transmembrane temperature difference. it was found that, under non-isothermal conditions and keeping constant the average temperature of the bioreactor, the enzyme reaction rate linearly increased with the increase of the temperature difference. (c) 2008 Elsevier B.V. All rights reserved.
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