Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste
The adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW), was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS...
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MDPI AG
2023-09-01
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| Online Access: | https://www.mdpi.com/2073-4344/13/10/1324 |
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| author | Carlos R. Llerena Suster Cynthia A. Fuentes Jorge E. Sambeth Carla José |
| author_facet | Carlos R. Llerena Suster Cynthia A. Fuentes Jorge E. Sambeth Carla José |
| author_sort | Carlos R. Llerena Suster |
| collection | DOAJ |
| description | The adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW), was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of <i>rac</i>-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g<sup>−1</sup> was obtained, achieving productivity of 0.298 mmol min<sup>−1</sup> mg<sup>−1</sup>. Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications. |
| first_indexed | 2024-03-10T21:21:30Z |
| format | Article |
| id | doaj.art-47b7be575bc14523825ffa9124e2be5f |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T21:21:30Z |
| publishDate | 2023-09-01 |
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| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-47b7be575bc14523825ffa9124e2be5f2023-11-19T16:00:54ZengMDPI AGCatalysts2073-43442023-09-011310132410.3390/catal13101324Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid WasteCarlos R. Llerena Suster0Cynthia A. Fuentes1Jorge E. Sambeth2Carla José3Center 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, CICPBA, La Plata B1900AJK, ArgentinaCenter for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, CICPBA, La Plata B1900AJK, ArgentinaCenter for Research and Development in Applied Sciences-Dr. Jorge J. Ronco, Universidad Nacional de La Plata, CONICET, CICPBA, La Plata B1900AJK, ArgentinaThe adsorption of the lipase B from <i>Candida antarctica</i> (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW), was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of <i>rac</i>-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g<sup>−1</sup> was obtained, achieving productivity of 0.298 mmol min<sup>−1</sup> mg<sup>−1</sup>. Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.https://www.mdpi.com/2073-4344/13/10/1324biocatalysisenzymespolyethylene terephthalatepolypropylenebis-(2-hydroxyethyl) terephthalategreen chemistry |
| spellingShingle | Carlos R. Llerena Suster Cynthia A. Fuentes Jorge E. Sambeth Carla José Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste Catalysts biocatalysis enzymes polyethylene terephthalate polypropylene bis-(2-hydroxyethyl) terephthalate green chemistry |
| title | Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste |
| title_full | Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste |
| title_fullStr | Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste |
| title_full_unstemmed | Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste |
| title_short | Immobilization of the Lipase B from <i>Candida antarctica</i> on Urban Solid Waste |
| title_sort | immobilization of the lipase b from i candida antarctica i on urban solid waste |
| topic | biocatalysis enzymes polyethylene terephthalate polypropylene bis-(2-hydroxyethyl) terephthalate green chemistry |
| url | https://www.mdpi.com/2073-4344/13/10/1324 |
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