Cargando…
Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine
In this study, we developed a new synthesis method for modifying activated carbon fibers (ACFs) by dopamine with oxidation-based self-polymerization (DA-ACFs). In addition, laccase was immobilized on the surface of unmodified ACFs (L-ACFs) and DA-ACFs (LDA-ACFs) via cross-linking after being incubat...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9079870/ https://www.ncbi.nlm.nih.gov/pubmed/35540792 http://dx.doi.org/10.1039/c8ra01265b |
_version_ | 1784702653813489664 |
---|---|
author | Zhang, Chencheng Gong, Lili Mao, Qinghui Han, Pingfang Lu, Xiaoping Qu, Jiangang |
author_facet | Zhang, Chencheng Gong, Lili Mao, Qinghui Han, Pingfang Lu, Xiaoping Qu, Jiangang |
author_sort | Zhang, Chencheng |
collection | PubMed |
description | In this study, we developed a new synthesis method for modifying activated carbon fibers (ACFs) by dopamine with oxidation-based self-polymerization (DA-ACFs). In addition, laccase was immobilized on the surface of unmodified ACFs (L-ACFs) and DA-ACFs (LDA-ACFs) via cross-linking after being incubated for 12 h at 5 °C. The surface composition and microstructure of the samples were characterized by scanning electron microscopy, X-ray photoelectron spectroscopy, attenuated total reflectance Fourier-transform infrared reflection and thermo-gravimetric analysis. The optimized laccase concentration for preparing the samples was 2.0 g L(−1). The results demonstrated that the successful poly-dopamine modification increased the catalytic abilities of the ACFs in terms of biocompatibility and hydrophilicity. Compared with free laccase, the immobilized laccase exhibited significantly higher relative activity over a pH range of 3.5–6.5 and a temperature range of 30–60 °C; the thermo-stability increased, and 50% relative activity of the LDA-ACFs remained after 5 h at 55 °C. After six cycles of reuse, the relative activity of LDA-ACFs remained ≥60%, compared to 40% activity remaining for L-ACFs, and long-term storage stability was demonstrated. Moreover, the kinetic parameters (K(m)) of the two immobilized laccases were both higher than that of free laccase, whereas the maximum velocities (V(max)) were lower. These results indicate that the DA-ACFs are economical, simple, and efficient carries for enzyme immobilization, and can be suitable for further biotechnology and environmental applications. |
format | Online Article Text |
id | pubmed-9079870 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-90798702022-05-09 Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine Zhang, Chencheng Gong, Lili Mao, Qinghui Han, Pingfang Lu, Xiaoping Qu, Jiangang RSC Adv Chemistry In this study, we developed a new synthesis method for modifying activated carbon fibers (ACFs) by dopamine with oxidation-based self-polymerization (DA-ACFs). In addition, laccase was immobilized on the surface of unmodified ACFs (L-ACFs) and DA-ACFs (LDA-ACFs) via cross-linking after being incubated for 12 h at 5 °C. The surface composition and microstructure of the samples were characterized by scanning electron microscopy, X-ray photoelectron spectroscopy, attenuated total reflectance Fourier-transform infrared reflection and thermo-gravimetric analysis. The optimized laccase concentration for preparing the samples was 2.0 g L(−1). The results demonstrated that the successful poly-dopamine modification increased the catalytic abilities of the ACFs in terms of biocompatibility and hydrophilicity. Compared with free laccase, the immobilized laccase exhibited significantly higher relative activity over a pH range of 3.5–6.5 and a temperature range of 30–60 °C; the thermo-stability increased, and 50% relative activity of the LDA-ACFs remained after 5 h at 55 °C. After six cycles of reuse, the relative activity of LDA-ACFs remained ≥60%, compared to 40% activity remaining for L-ACFs, and long-term storage stability was demonstrated. Moreover, the kinetic parameters (K(m)) of the two immobilized laccases were both higher than that of free laccase, whereas the maximum velocities (V(max)) were lower. These results indicate that the DA-ACFs are economical, simple, and efficient carries for enzyme immobilization, and can be suitable for further biotechnology and environmental applications. The Royal Society of Chemistry 2018-04-17 /pmc/articles/PMC9079870/ /pubmed/35540792 http://dx.doi.org/10.1039/c8ra01265b Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Zhang, Chencheng Gong, Lili Mao, Qinghui Han, Pingfang Lu, Xiaoping Qu, Jiangang Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title | Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title_full | Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title_fullStr | Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title_full_unstemmed | Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title_short | Laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
title_sort | laccase immobilization and surface modification of activated carbon fibers by bio-inspired poly-dopamine |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9079870/ https://www.ncbi.nlm.nih.gov/pubmed/35540792 http://dx.doi.org/10.1039/c8ra01265b |
work_keys_str_mv | AT zhangchencheng laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine AT gonglili laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine AT maoqinghui laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine AT hanpingfang laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine AT luxiaoping laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine AT qujiangang laccaseimmobilizationandsurfacemodificationofactivatedcarbonfibersbybioinspiredpolydopamine |