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Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning
Controlling surface–protein interaction during wastewater treatment is the key motivation for developing functionally modified membranes. A new biocatalytic thermo-responsive poly vinylidene fluoride (PVDF)/nylon-6,6/poly(N-isopropylacrylamide)(PNIPAAm) ultrafiltration membrane was fabricated to ach...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6161312/ https://www.ncbi.nlm.nih.gov/pubmed/30235868 http://dx.doi.org/10.3390/membranes8030085 |
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author | Vanangamudi, Anbharasi Dumée, Ludovic F. Duke, Mikel C. Yang, Xing |
author_facet | Vanangamudi, Anbharasi Dumée, Ludovic F. Duke, Mikel C. Yang, Xing |
author_sort | Vanangamudi, Anbharasi |
collection | PubMed |
description | Controlling surface–protein interaction during wastewater treatment is the key motivation for developing functionally modified membranes. A new biocatalytic thermo-responsive poly vinylidene fluoride (PVDF)/nylon-6,6/poly(N-isopropylacrylamide)(PNIPAAm) ultrafiltration membrane was fabricated to achieve dual functionality of protein-digestion and thermo-responsive self-cleaning. The PVDF/nylon-6,6/PNIPAAm composite membranes were constructed by integrating a hydrophobic PVDF cast layer and hydrophilic nylon-6,6/PNIPAAm nanofiber layer on to which trypsin was covalently immobilized. The enzyme immobilization density on the membrane surface decreased with increasing PNIPAAm concentration, due to the decreased number of amine functional sites. An ultrafiltration study was performed using the synthetic model solution containing BSA/NaCl/CaCl(2,) where the PNIPAAm containing biocatalytic membranes demonstrated a combined effect of enzymatic and thermo-switchable self-cleaning. The membrane without PNIPAAm revealed superior fouling resistance and self-cleaning with an R(PD) of 22%, compared to membranes with 2 and 4 wt % PNIPAAm with 26% and 33% R(PD), respectively, after an intermediate temperature cleaning at 50 °C, indicating that higher enzyme density offers more efficient self-cleaning than the combined effect of enzyme and PNIPAAm at low concentration. The conformational volume phase transition of PNIPAAm did not affect the stability of immobilized trypsin on membrane surfaces. Such novel surface engineering design offer a promising route to mitigate surface–protein contamination in wastewater applications. |
format | Online Article Text |
id | pubmed-6161312 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-61613122018-09-28 Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning Vanangamudi, Anbharasi Dumée, Ludovic F. Duke, Mikel C. Yang, Xing Membranes (Basel) Article Controlling surface–protein interaction during wastewater treatment is the key motivation for developing functionally modified membranes. A new biocatalytic thermo-responsive poly vinylidene fluoride (PVDF)/nylon-6,6/poly(N-isopropylacrylamide)(PNIPAAm) ultrafiltration membrane was fabricated to achieve dual functionality of protein-digestion and thermo-responsive self-cleaning. The PVDF/nylon-6,6/PNIPAAm composite membranes were constructed by integrating a hydrophobic PVDF cast layer and hydrophilic nylon-6,6/PNIPAAm nanofiber layer on to which trypsin was covalently immobilized. The enzyme immobilization density on the membrane surface decreased with increasing PNIPAAm concentration, due to the decreased number of amine functional sites. An ultrafiltration study was performed using the synthetic model solution containing BSA/NaCl/CaCl(2,) where the PNIPAAm containing biocatalytic membranes demonstrated a combined effect of enzymatic and thermo-switchable self-cleaning. The membrane without PNIPAAm revealed superior fouling resistance and self-cleaning with an R(PD) of 22%, compared to membranes with 2 and 4 wt % PNIPAAm with 26% and 33% R(PD), respectively, after an intermediate temperature cleaning at 50 °C, indicating that higher enzyme density offers more efficient self-cleaning than the combined effect of enzyme and PNIPAAm at low concentration. The conformational volume phase transition of PNIPAAm did not affect the stability of immobilized trypsin on membrane surfaces. Such novel surface engineering design offer a promising route to mitigate surface–protein contamination in wastewater applications. MDPI 2018-09-19 /pmc/articles/PMC6161312/ /pubmed/30235868 http://dx.doi.org/10.3390/membranes8030085 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Vanangamudi, Anbharasi Dumée, Ludovic F. Duke, Mikel C. Yang, Xing Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title | Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title_full | Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title_fullStr | Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title_full_unstemmed | Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title_short | Dual Functional Ultrafiltration Membranes with Enzymatic Digestion and Thermo-Responsivity for Protein Self-Cleaning |
title_sort | dual functional ultrafiltration membranes with enzymatic digestion and thermo-responsivity for protein self-cleaning |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6161312/ https://www.ncbi.nlm.nih.gov/pubmed/30235868 http://dx.doi.org/10.3390/membranes8030085 |
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