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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...

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Autores principales: Zhang, Jie, Li, Fukun, Wang, Ruiqi, Tan, Xuemei, Hagedoorn, Peter-Leon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2020
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]
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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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