Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface
The design of interfaces that selectively react with molecules to transform them into compounds of industrial interest is an emerging area of research. An example of such reactions is the hydrolytic conversion of ester-based molecules to lipids and alcohols, which is of interest to the food, and pha...
Published in: | Colloids and Surfaces B: Biointerfaces |
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/ http://www.ncbi.nlm.nih.gov/pubmed/31404792 https://doi.org/10.1016/j.colsurfb.2019.110418 |
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ftpubmed:oai:pubmedcentral.nih.gov:6815258 2023-05-15T13:58:32+02:00 Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface Pazol, Jessika Vázquez, Adriana Nicolau, Eduardo 2019-08-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/ http://www.ncbi.nlm.nih.gov/pubmed/31404792 https://doi.org/10.1016/j.colsurfb.2019.110418 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/ http://www.ncbi.nlm.nih.gov/pubmed/31404792 http://dx.doi.org/10.1016/j.colsurfb.2019.110418 Colloids Surf B Biointerfaces Article Text 2019 ftpubmed https://doi.org/10.1016/j.colsurfb.2019.110418 2020-11-08T01:19:47Z The design of interfaces that selectively react with molecules to transform them into compounds of industrial interest is an emerging area of research. An example of such reactions is the hydrolytic conversion of ester-based molecules to lipids and alcohols, which is of interest to the food, and pharmaceutical industries. In this study, a functional bio-interfaced layer was designed to hydrolyze 4-nitrophenyl acetate (pNPA) and Ricinus Communis (castor) oil rich in triglycerides using lipase b from Candida antarctica (CALB, EC 3.1.1.3). The attachment of CALB was performed via non-covalent immobilization over a polymer film of vertically aligned cylinders that resulted from the self-assembly of the di-block copolymer polystyrene-block-poly(4-vinyl pyridine) (PS-b-P4VP). This polymer-lipase model will serve as the groundwork for the design of further bioactive layers for separation applications requiring similar hydrolytic processes. Results from the fabricated functional bio-interfaced material include cylinders with featured pore size of 19 nm, d spacing of 34 nm, and ca. 40 nm of thickness. The polymer-enzyme layers were physically characterized using AFM, XPS, and FTIR. The immobilized enzyme was able to retain 91% of the initial enzymatic activity when using 4-nitrophenyl acetate (pNPA) and 78% when exposed to triglycerides from castor oil. Text Antarc* Antarctica antartic* PubMed Central (PMC) Colloids and Surfaces B: Biointerfaces 183 110418 |
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Article Pazol, Jessika Vázquez, Adriana Nicolau, Eduardo Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
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Article |
description |
The design of interfaces that selectively react with molecules to transform them into compounds of industrial interest is an emerging area of research. An example of such reactions is the hydrolytic conversion of ester-based molecules to lipids and alcohols, which is of interest to the food, and pharmaceutical industries. In this study, a functional bio-interfaced layer was designed to hydrolyze 4-nitrophenyl acetate (pNPA) and Ricinus Communis (castor) oil rich in triglycerides using lipase b from Candida antarctica (CALB, EC 3.1.1.3). The attachment of CALB was performed via non-covalent immobilization over a polymer film of vertically aligned cylinders that resulted from the self-assembly of the di-block copolymer polystyrene-block-poly(4-vinyl pyridine) (PS-b-P4VP). This polymer-lipase model will serve as the groundwork for the design of further bioactive layers for separation applications requiring similar hydrolytic processes. Results from the fabricated functional bio-interfaced material include cylinders with featured pore size of 19 nm, d spacing of 34 nm, and ca. 40 nm of thickness. The polymer-enzyme layers were physically characterized using AFM, XPS, and FTIR. The immobilized enzyme was able to retain 91% of the initial enzymatic activity when using 4-nitrophenyl acetate (pNPA) and 78% when exposed to triglycerides from castor oil. |
format |
Text |
author |
Pazol, Jessika Vázquez, Adriana Nicolau, Eduardo |
author_facet |
Pazol, Jessika Vázquez, Adriana Nicolau, Eduardo |
author_sort |
Pazol, Jessika |
title |
Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
title_short |
Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
title_full |
Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
title_fullStr |
Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
title_full_unstemmed |
Characterization of non-covalent immobilized Candida antartica lipase b over PS-b-P4VP as a model bio-reactive porous interface |
title_sort |
characterization of non-covalent immobilized candida antartica lipase b over ps-b-p4vp as a model bio-reactive porous interface |
publishDate |
2019 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/ http://www.ncbi.nlm.nih.gov/pubmed/31404792 https://doi.org/10.1016/j.colsurfb.2019.110418 |
genre |
Antarc* Antarctica antartic* |
genre_facet |
Antarc* Antarctica antartic* |
op_source |
Colloids Surf B Biointerfaces |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815258/ http://www.ncbi.nlm.nih.gov/pubmed/31404792 http://dx.doi.org/10.1016/j.colsurfb.2019.110418 |
op_doi |
https://doi.org/10.1016/j.colsurfb.2019.110418 |
container_title |
Colloids and Surfaces B: Biointerfaces |
container_volume |
183 |
container_start_page |
110418 |
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1766266884680843264 |