Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub>
The adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over nanostructured SiO<sub>2</sub> (Ns SiO<sub>2</sub> from now on) with and without the addition of polyols (sorbitol and glycerol) was investigated. The isotherms of adsorption made it possibl...
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MDPI AG
2023-03-01
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| Series: | Catalysts |
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| Online Access: | https://www.mdpi.com/2073-4344/13/3/625 |
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| author | Carlos R. Llerena Suster María V. Toledo Silvana R. Matkovic Susana R. Morcelle Laura E. Briand |
| author_facet | Carlos R. Llerena Suster María V. Toledo Silvana R. Matkovic Susana R. Morcelle Laura E. Briand |
| author_sort | Carlos R. Llerena Suster |
| collection | DOAJ |
| description | The adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over nanostructured SiO<sub>2</sub> (Ns SiO<sub>2</sub> from now on) with and without the addition of polyols (sorbitol and glycerol) was investigated. The isotherms of adsorption made it possible to establish that the maximum dispersion limit was 0.029 µmol of protein per surface area unit of Ns SiO<sub>2</sub> (29.4 mg per 100 mg of support), which was reached in 30 min of exposure. The studies through SDS-PAGE of the immobilization solutions and infrared spectroscopy of the prepared solids determined that CALB (from a commercial extract) is selectively adsorbed, and its secondary structure distribution is thus modified. Its biocatalytic activity was corroborated through the kinetic resolution of rac-ibuprofen. Conversions of up to 70% and 52% enantiomeric excess toward <i>S</i>-ibuprofen in 24 h of reaction at 45 °C were achieved. The biocatalytic performance increased with the increase in protein loading until it leveled off at 0.021 µmol.m<sup>−2</sup>, reaching 0.6 µmol.min<sup>−1</sup>. The biocatalyst containing the lipase at the maximum dispersion limit and co-adsorbed polyols presented the best catalytic performance in the kinetic resolution of rac-ibuprofen, an improved thermal resistance (up to 70 °C), and stability under long-term storage (more than 2 years). |
| first_indexed | 2024-03-11T06:48:11Z |
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| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-11T06:48:11Z |
| publishDate | 2023-03-01 |
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| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-f613eab6fa7b4bf6b585af9caa5bc47c2023-11-17T10:12:06ZengMDPI AGCatalysts2073-43442023-03-0113362510.3390/catal13030625Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub>Carlos R. Llerena Suster0María V. Toledo1Silvana R. Matkovic2Susana R. Morcelle3Laura E. Briand4Center for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, La Plata B1900AJK, ArgentinaCenter for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, La Plata B1900AJK, ArgentinaCenter for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, La Plata B1900AJK, ArgentinaCenter for Research in Vegetable Proteins (CIPROVE), Department of Biological Sciences, Faculty of Exact Sciences, The National University of La Plata-Associated Center CIC, La Plata B1900AFW, ArgentinaCenter for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, La Plata B1900AJK, ArgentinaThe adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over nanostructured SiO<sub>2</sub> (Ns SiO<sub>2</sub> from now on) with and without the addition of polyols (sorbitol and glycerol) was investigated. The isotherms of adsorption made it possible to establish that the maximum dispersion limit was 0.029 µmol of protein per surface area unit of Ns SiO<sub>2</sub> (29.4 mg per 100 mg of support), which was reached in 30 min of exposure. The studies through SDS-PAGE of the immobilization solutions and infrared spectroscopy of the prepared solids determined that CALB (from a commercial extract) is selectively adsorbed, and its secondary structure distribution is thus modified. Its biocatalytic activity was corroborated through the kinetic resolution of rac-ibuprofen. Conversions of up to 70% and 52% enantiomeric excess toward <i>S</i>-ibuprofen in 24 h of reaction at 45 °C were achieved. The biocatalytic performance increased with the increase in protein loading until it leveled off at 0.021 µmol.m<sup>−2</sup>, reaching 0.6 µmol.min<sup>−1</sup>. The biocatalyst containing the lipase at the maximum dispersion limit and co-adsorbed polyols presented the best catalytic performance in the kinetic resolution of rac-ibuprofen, an improved thermal resistance (up to 70 °C), and stability under long-term storage (more than 2 years).https://www.mdpi.com/2073-4344/13/3/625lipasesnanostructured SiO<sub>2</sub>biocatalysisimmobilizationadsorptionkinetic resolution |
| spellingShingle | Carlos R. Llerena Suster María V. Toledo Silvana R. Matkovic Susana R. Morcelle Laura E. Briand Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> Catalysts lipases nanostructured SiO<sub>2</sub> biocatalysis immobilization adsorption kinetic resolution |
| title | Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> |
| title_full | Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> |
| title_fullStr | Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> |
| title_full_unstemmed | Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> |
| title_short | Rational Design of a Biocatalyst Based on Immobilized CALB onto Nanostructured SiO<sub>2</sub> |
| title_sort | rational design of a biocatalyst based on immobilized calb onto nanostructured sio sub 2 sub |
| topic | lipases nanostructured SiO<sub>2</sub> biocatalysis immobilization adsorption kinetic resolution |
| url | https://www.mdpi.com/2073-4344/13/3/625 |
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