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 ® TL (TLL-IM) (lipase from Thermomyces lanuginose ), Lipo...
Published in: | Molecules |
---|---|
Main Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
MDPI AG
2022
|
Subjects: | |
Online Access: | https://doi.org/10.3390/molecules27144486 https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6 |
_version_ | 1821606647886249984 |
---|---|
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 | Directory of Open Access Journals: DOAJ Articles |
container_issue | 14 |
container_start_page | 4486 |
container_title | Molecules |
container_volume | 27 |
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 ® TL (TLL-IM) (lipase from Thermomyces lanuginose ), Lipozyme ® 435 (L435) (lipase B from Candida antarctica ), Lipozyme ® RM (RML-IM), and LipuraSelect (LS-IM) (both from lipase from Rhizomucor miehei ). 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 R - or S - methyl mandelate). Enantiospecificity was also drastically altered after these modifications, e.g., LS-IM increased the activity versus the R isomer while decreasing the activity versus the S 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. |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftdoajarticles:oai:doaj.org/article:cc44dc19cfd24e9fae8dded43e9b99c6 |
institution | Open Polar |
language | English |
op_collection_id | ftdoajarticles |
op_doi | https://doi.org/10.3390/molecules27144486 |
op_relation | https://www.mdpi.com/1420-3049/27/14/4486 https://doaj.org/toc/1420-3049 doi:10.3390/molecules27144486 1420-3049 https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6 |
op_source | Molecules, Vol 27, Iss 4486, p 4486 (2022) |
publishDate | 2022 |
publisher | MDPI AG |
record_format | openpolar |
spelling | ftdoajarticles:oai:doaj.org/article:cc44dc19cfd24e9fae8dded43e9b99c6 2025-01-16T19:09:06+00:00 Tuning Immobilized Commercial Lipase Preparations Features by Simple Treatment with Metallic Phosphate Salts José R. Guimarães Diego Carballares Paulo W. Tardioli Javier Rocha-Martin Roberto Fernandez-Lafuente 2022-07-01T00:00:00Z https://doi.org/10.3390/molecules27144486 https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6 EN eng MDPI AG https://www.mdpi.com/1420-3049/27/14/4486 https://doaj.org/toc/1420-3049 doi:10.3390/molecules27144486 1420-3049 https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6 Molecules, Vol 27, Iss 4486, p 4486 (2022) solid phase enzyme mineralization nanoflowers immobilized lipases enzyme specificity enzyme stability Organic chemistry QD241-441 article 2022 ftdoajarticles https://doi.org/10.3390/molecules27144486 2022-12-31T01:04:04Z 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 ® TL (TLL-IM) (lipase from Thermomyces lanuginose ), Lipozyme ® 435 (L435) (lipase B from Candida antarctica ), Lipozyme ® RM (RML-IM), and LipuraSelect (LS-IM) (both from lipase from Rhizomucor miehei ). 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 R - or S - methyl mandelate). Enantiospecificity was also drastically altered after these modifications, e.g., LS-IM increased the activity versus the R isomer while decreasing the activity versus the S 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. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Molecules 27 14 4486 |
spellingShingle | solid phase enzyme mineralization nanoflowers immobilized lipases enzyme specificity enzyme stability Organic chemistry QD241-441 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 |
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 Organic chemistry QD241-441 |
topic_facet | solid phase enzyme mineralization nanoflowers immobilized lipases enzyme specificity enzyme stability Organic chemistry QD241-441 |
url | https://doi.org/10.3390/molecules27144486 https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6 |