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Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization
Laccase is a versatile multicopper oxidase that holds great promise for many biotechnological applications. For such applications, it is essential to explore good biocatalytic systems for high activity and recyclability. The feasibility of membrane enclosed enzymatic catalysis (MEEC) for enzyme recy...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6987272/ https://www.ncbi.nlm.nih.gov/pubmed/31993852 http://dx.doi.org/10.1186/s13568-020-0955-6 |
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author | Zhang, Jie Li, Fukun Wang, Ruiqi Tan, Xuemei Hagedoorn, Peter-Leon |
author_facet | Zhang, Jie Li, Fukun Wang, Ruiqi Tan, Xuemei Hagedoorn, Peter-Leon |
author_sort | Zhang, Jie |
collection | PubMed |
description | Laccase is a versatile multicopper oxidase that holds great promise for many biotechnological applications. For such applications, it is essential to explore good biocatalytic systems for high activity and recyclability. The feasibility of membrane enclosed enzymatic catalysis (MEEC) for enzyme recycling with laccase was evaluated. The dialysis membrane enclosed laccase catalysis (DMELC) was tested for the conversion of the non-phenolic model substrate 2,2′-Azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS). Trametes versicolor laccase was found to be completely retained by the dialysis membrane during the process. The ABTS total conversion after DMELC reached the same values as the batch reaction of the enzyme in solution. The efficiency of DMELC conversion of ABTS under different process conditions including shaking speed, temperature, ABTS concentration and pH was investigated. The repetitive dialysis minimally affected the activity and the protein content of the enclosed laccase. DMELC retained 70.3 ± 0.8% of its initial conversion after 5 cycles. The usefulness of MEEC extends to other enzymes with the benefit of superior activity of an enzyme in solution and the recyclability which is normally only obtained with immobilized enzymes. [Image: see text] |
format | Online Article Text |
id | pubmed-6987272 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-69872722020-02-11 Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization Zhang, Jie Li, Fukun Wang, Ruiqi Tan, Xuemei Hagedoorn, Peter-Leon AMB Express Original Article Laccase is a versatile multicopper oxidase that holds great promise for many biotechnological applications. For such applications, it is essential to explore good biocatalytic systems for high activity and recyclability. The feasibility of membrane enclosed enzymatic catalysis (MEEC) for enzyme recycling with laccase was evaluated. The dialysis membrane enclosed laccase catalysis (DMELC) was tested for the conversion of the non-phenolic model substrate 2,2′-Azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS). Trametes versicolor laccase was found to be completely retained by the dialysis membrane during the process. The ABTS total conversion after DMELC reached the same values as the batch reaction of the enzyme in solution. The efficiency of DMELC conversion of ABTS under different process conditions including shaking speed, temperature, ABTS concentration and pH was investigated. The repetitive dialysis minimally affected the activity and the protein content of the enclosed laccase. DMELC retained 70.3 ± 0.8% of its initial conversion after 5 cycles. The usefulness of MEEC extends to other enzymes with the benefit of superior activity of an enzyme in solution and the recyclability which is normally only obtained with immobilized enzymes. [Image: see text] Springer Berlin Heidelberg 2020-01-28 /pmc/articles/PMC6987272/ /pubmed/31993852 http://dx.doi.org/10.1186/s13568-020-0955-6 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Original Article Zhang, Jie Li, Fukun Wang, Ruiqi Tan, Xuemei Hagedoorn, Peter-Leon Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title | Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title_full | Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title_fullStr | Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title_full_unstemmed | Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title_short | Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
title_sort | dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6987272/ https://www.ncbi.nlm.nih.gov/pubmed/31993852 http://dx.doi.org/10.1186/s13568-020-0955-6 |
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