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Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process

In this work, new M(x)O(y)/fucoidan hybrid systems were fabricated and applied in lipase immobilization. Magnesium (MgO) and zirconium (ZrO(2)) oxides were used as M(x)O(y) inorganic matrices. In the first step, the proposed oxides were functionalized with fucoidan from Fucus vesiculosus (Fuc). The...

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Autores principales: Kołodziejczak-Radzimska, Agnieszka, Bielejewski, Michał, Biadasz, Andrzej, Jesionowski, Teofil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068721/
https://www.ncbi.nlm.nih.gov/pubmed/35508694
http://dx.doi.org/10.1038/s41598-022-11319-0
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author Kołodziejczak-Radzimska, Agnieszka
Bielejewski, Michał
Biadasz, Andrzej
Jesionowski, Teofil
author_facet Kołodziejczak-Radzimska, Agnieszka
Bielejewski, Michał
Biadasz, Andrzej
Jesionowski, Teofil
author_sort Kołodziejczak-Radzimska, Agnieszka
collection PubMed
description In this work, new M(x)O(y)/fucoidan hybrid systems were fabricated and applied in lipase immobilization. Magnesium (MgO) and zirconium (ZrO(2)) oxides were used as M(x)O(y) inorganic matrices. In the first step, the proposed oxides were functionalized with fucoidan from Fucus vesiculosus (Fuc). The obtained MgO/Fuc and ZrO(2)/Fuc hybrids were characterized by means of spectroscopic analyses, including Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, and nuclear magnetic resonance. Additionally, thermogravimetric analysis was performed to determine the thermal stability of the hybrids. Based on the results, the mechanism of interaction between the oxide supports and fucoidan was also determined. Furthermore, the fabricated M(x)O(y)/fucoidan hybrid materials were used as supports for the immobilization of lipase from Aspergillus niger, and a model reaction (transformation of p-nitrophenyl palmitate to p-nitrophenol) was performed to determine the catalytic activity of the proposed biocatalytic system. In that reaction, the immobilized lipase exhibited high apparent and specific activity (145.5 U/g(catalyst) and 1.58 U/mg(enzyme) for lipase immobilized on MgO/Fuc; 144.0 U/g(catalyst) and 2.03 U/mg(enzyme) for lipase immobilized on ZrO(2)/Fuc). The immobilization efficiency was also confirmed using spectroscopic analyses (FTIR and XPS) and confocal microscopy.
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spelling pubmed-90687212022-05-05 Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process Kołodziejczak-Radzimska, Agnieszka Bielejewski, Michał Biadasz, Andrzej Jesionowski, Teofil Sci Rep Article In this work, new M(x)O(y)/fucoidan hybrid systems were fabricated and applied in lipase immobilization. Magnesium (MgO) and zirconium (ZrO(2)) oxides were used as M(x)O(y) inorganic matrices. In the first step, the proposed oxides were functionalized with fucoidan from Fucus vesiculosus (Fuc). The obtained MgO/Fuc and ZrO(2)/Fuc hybrids were characterized by means of spectroscopic analyses, including Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, and nuclear magnetic resonance. Additionally, thermogravimetric analysis was performed to determine the thermal stability of the hybrids. Based on the results, the mechanism of interaction between the oxide supports and fucoidan was also determined. Furthermore, the fabricated M(x)O(y)/fucoidan hybrid materials were used as supports for the immobilization of lipase from Aspergillus niger, and a model reaction (transformation of p-nitrophenyl palmitate to p-nitrophenol) was performed to determine the catalytic activity of the proposed biocatalytic system. In that reaction, the immobilized lipase exhibited high apparent and specific activity (145.5 U/g(catalyst) and 1.58 U/mg(enzyme) for lipase immobilized on MgO/Fuc; 144.0 U/g(catalyst) and 2.03 U/mg(enzyme) for lipase immobilized on ZrO(2)/Fuc). The immobilization efficiency was also confirmed using spectroscopic analyses (FTIR and XPS) and confocal microscopy. Nature Publishing Group UK 2022-05-04 /pmc/articles/PMC9068721/ /pubmed/35508694 http://dx.doi.org/10.1038/s41598-022-11319-0 Text en © The Author(s) 2022, corrected publication 2022 https://creativecommons.org/licenses/by/4.0/Open Access This 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/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Kołodziejczak-Radzimska, Agnieszka
Bielejewski, Michał
Biadasz, Andrzej
Jesionowski, Teofil
Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title_full Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title_fullStr Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title_full_unstemmed Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title_short Evaluation of M(x)O(y)/fucoidan hybrid system and their application in lipase immobilization process
title_sort evaluation of m(x)o(y)/fucoidan hybrid system and their application in lipase immobilization process
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068721/
https://www.ncbi.nlm.nih.gov/pubmed/35508694
http://dx.doi.org/10.1038/s41598-022-11319-0
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