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...

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Published in:Molecules
Main Authors: José R. Guimarães, Diego Carballares, Paulo W. Tardioli, Javier Rocha-Martin, Roberto Fernandez-Lafuente
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2022
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Online Access:https://doi.org/10.3390/molecules27144486
https://doaj.org/article/cc44dc19cfd24e9fae8dded43e9b99c6
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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 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.
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doi:10.3390/molecules27144486
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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