Additives enhancing the catalytic properties of lipase from Burkholderia cepacia immobilized on mixed-function-grafted mesoporous silica gel.
| Autor: | Abaházi E; Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, Hungary. abahazi.emese@mail.bme.hu., Boros Z; Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, Hungary. zoltan.boros@synbiocat.com., Poppe L; Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, Hungary. poppe@mail.bme.hu. |
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| Jazyk: | angličtina |
| Zdroj: | Molecules (Basel, Switzerland) [Molecules] 2014 Jul 08; Vol. 19 (7), pp. 9818-37. Date of Electronic Publication: 2014 Jul 08. |
| DOI: | 10.3390/molecules19079818 |
| Abstrakt: | Effects of various additives on the lipase from Burkholderia cepacia (BcL) immobilized on mixed-function-grafted mesoporous silica gel support by hydrophobic adsorption and covalent attachment were investigated. Catalytic properties of the immobilized biocatalysts were characterized in kinetic resolution of racemic 1-phenylethanol (rac-1a) and 1-(thiophen-2-yl)ethan-1-ol (rac-1b). Screening of more than 40 additives showed significantly enhanced productivity of immobilized BcL with several additives such as PEGs, oleic acid and polyvinyl alcohol. Effects of substrate concentration and temperature between 0-100 °C on kinetic resolution of rac-1a were studied with the best adsorbed BcLs containing PEG 20 k or PVA 18-88 additives in continuous-flow packed-bed reactor. The optimum temperature of lipase activity for BcL co-immobilized with PEG 20k found at around 30 °C determined in the continuous-flow system increased remarkably to around 80 °C for BcL co-immobilized with PVA 18-88. |
| Databáze: | MEDLINE |
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