Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts
Four commercial immobilized lipases biocatalysts have been submitted to modifications with different metal (zinc, cobalt or copper) phosphates to check the effects of this modification on enzyme features. The lipase preparations were Lipozyme<sup>®</sup>TL (TLL-IM) (lipase from <i>...
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MDPI AG
2022-07-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/27/14/4486 |
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| author | José R. Guimarães Diego Carballares Paulo W. Tardioli Javier Rocha-Martin Roberto Fernandez-Lafuente |
| author_facet | José R. Guimarães Diego Carballares Paulo W. Tardioli Javier Rocha-Martin Roberto Fernandez-Lafuente |
| author_sort | José R. Guimarães |
| collection | DOAJ |
| description | Four commercial immobilized lipases biocatalysts have been submitted to modifications with different metal (zinc, cobalt or copper) phosphates to check the effects of this modification on enzyme features. The lipase preparations were Lipozyme<sup>®</sup>TL (TLL-IM) (lipase from <i>Thermomyces lanuginose</i>), Lipozyme<sup>®</sup>435 (L435) (lipase B from <i>Candida antarctica</i>), Lipozyme<sup>®</sup>RM (RML-IM), and LipuraSelect (LS-IM) (both from lipase from <i>Rhizomucor miehei</i>). The modifications greatly altered enzyme specificity, increasing the activity versus some substrates (e.g., TLL-IM modified with zinc phosphate in hydrolysis of triacetin) while decreasing the activity versus other substrates (the same preparation in activity versus <i>R</i>- or <i>S</i>- methyl mandelate). Enantiospecificity was also drastically altered after these modifications, e.g., LS-IM increased the activity versus the <i>R</i> isomer while decreasing the activity versus the <i>S</i> isomer when treated with copper phosphate. Regarding the enzyme stability, it was significantly improved using octyl-agarose-lipases. Using all these commercial biocatalysts, no significant positive effects were found; in fact, a decrease in enzyme stability was usually detected. The results point towards the possibility of a battery of biocatalysts, including many different metal phosphates and immobilization protocols, being a good opportunity to tune enzyme features, increasing the possibilities of having biocatalysts that may be suitable for a specific process. |
| first_indexed | 2024-03-09T13:17:50Z |
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| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T13:17:50Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
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| series | Molecules |
| spelling | doaj.art-cc44dc19cfd24e9fae8dded43e9b99c62023-11-30T21:33:40ZengMDPI AGMolecules1420-30492022-07-012714448610.3390/molecules27144486Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate SaltsJosé R. Guimarães0Diego Carballares1Paulo W. Tardioli2Javier Rocha-Martin3Roberto Fernandez-Lafuente4Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, SpainDepartamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, SpainLaboratory of Enzyme Technologies (LabEnz), Department of Chemical Engineering, Federal University of São Carlos (DEQ/UFSCar), Rod. Washington Luís, km 235, São Carlos 13565-905, BrazilDepartment of Biochemistry and Molecular Biology, Faculty of Biology, Complutense University of Madrid, José Antonio Novais 12, 28040 Madrid, SpainDepartamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, SpainFour commercial immobilized lipases biocatalysts have been submitted to modifications with different metal (zinc, cobalt or copper) phosphates to check the effects of this modification on enzyme features. The lipase preparations were Lipozyme<sup>®</sup>TL (TLL-IM) (lipase from <i>Thermomyces lanuginose</i>), Lipozyme<sup>®</sup>435 (L435) (lipase B from <i>Candida antarctica</i>), Lipozyme<sup>®</sup>RM (RML-IM), and LipuraSelect (LS-IM) (both from lipase from <i>Rhizomucor miehei</i>). The modifications greatly altered enzyme specificity, increasing the activity versus some substrates (e.g., TLL-IM modified with zinc phosphate in hydrolysis of triacetin) while decreasing the activity versus other substrates (the same preparation in activity versus <i>R</i>- or <i>S</i>- methyl mandelate). Enantiospecificity was also drastically altered after these modifications, e.g., LS-IM increased the activity versus the <i>R</i> isomer while decreasing the activity versus the <i>S</i> isomer when treated with copper phosphate. Regarding the enzyme stability, it was significantly improved using octyl-agarose-lipases. Using all these commercial biocatalysts, no significant positive effects were found; in fact, a decrease in enzyme stability was usually detected. The results point towards the possibility of a battery of biocatalysts, including many different metal phosphates and immobilization protocols, being a good opportunity to tune enzyme features, increasing the possibilities of having biocatalysts that may be suitable for a specific process.https://www.mdpi.com/1420-3049/27/14/4486solid phase enzyme mineralizationnanoflowersimmobilized lipasesenzyme specificityenzyme stability |
| spellingShingle | José R. Guimarães Diego Carballares Paulo W. Tardioli Javier Rocha-Martin Roberto Fernandez-Lafuente Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts Molecules solid phase enzyme mineralization nanoflowers immobilized lipases enzyme specificity enzyme stability |
| title | Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts |
| title_full | Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts |
| title_fullStr | Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts |
| title_full_unstemmed | Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts |
| title_short | Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts |
| title_sort | tuning immobilized commercial lipase preparations features by simple treatment with metallic phosphate salts |
| topic | solid phase enzyme mineralization nanoflowers immobilized lipases enzyme specificity enzyme stability |
| url | https://www.mdpi.com/1420-3049/27/14/4486 |
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