Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel
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 resol...
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-07-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/19/7/9818 |
| _version_ | 1819180699906736128 |
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| author | Emese Abaházi Zoltán Boros László Poppe |
| author_facet | Emese Abaházi Zoltán Boros László Poppe |
| author_sort | Emese Abaházi |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T22:18:30Z |
| format | Article |
| id | doaj.art-c5b0e7c304c640dabf202eef709a2c4b |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-22T22:18:30Z |
| publishDate | 2014-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-c5b0e7c304c640dabf202eef709a2c4b2022-12-21T18:10:43ZengMDPI AGMolecules1420-30492014-07-011979818983710.3390/molecules19079818molecules19079818Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica GelEmese Abaházi0Zoltán Boros1László Poppe2Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, HungaryDepartment of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, HungaryEffects 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.http://www.mdpi.com/1420-3049/19/7/9818silica gelBurkholderia cepacia lipaseenzyme immobilizationadsorptionactivity enhancementadditivecontinuous-flow packed-bed reactor |
| spellingShingle | Emese Abaházi Zoltán Boros László Poppe Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel Molecules silica gel Burkholderia cepacia lipase enzyme immobilization adsorption activity enhancement additive continuous-flow packed-bed reactor |
| title | Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel |
| title_full | Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel |
| title_fullStr | Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel |
| title_full_unstemmed | Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel |
| title_short | Additives Enhancing the Catalytic Properties of Lipase from Burkholderia cepacia Immobilized on Mixed-Function-Grafted Mesoporous Silica Gel |
| title_sort | additives enhancing the catalytic properties of lipase from burkholderia cepacia immobilized on mixed function grafted mesoporous silica gel |
| topic | silica gel Burkholderia cepacia lipase enzyme immobilization adsorption activity enhancement additive continuous-flow packed-bed reactor |
| url | http://www.mdpi.com/1420-3049/19/7/9818 |
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