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Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement
The presence of sulfate groups in agar compromises the agar quality by affecting the crosslinking during gelling process. Some arylsulfatases can catalyze the hydrolysis of sulfate bonds in agar to improve the agar quality. Immobilized arylsulfatases prove beneficial advantages for their industrial...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8441490/ https://www.ncbi.nlm.nih.gov/pubmed/34532007 http://dx.doi.org/10.1002/fsn3.2446 |
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author | Zhang, Chenghao Jiang, Zedong Li, Hebin Ni, Hui Zheng, Mingjing Li, Qingbiao Zhu, Yanbing |
author_facet | Zhang, Chenghao Jiang, Zedong Li, Hebin Ni, Hui Zheng, Mingjing Li, Qingbiao Zhu, Yanbing |
author_sort | Zhang, Chenghao |
collection | PubMed |
description | The presence of sulfate groups in agar compromises the agar quality by affecting the crosslinking during gelling process. Some arylsulfatases can catalyze the hydrolysis of sulfate bonds in agar to improve the agar quality. Immobilized arylsulfatases prove beneficial advantages for their industrial applications. Here, a previously characterized mutant arylsulfatase K253H/H260L was immobilized on the synthesized magnetic Fe(3)O(4) nanoparticles after functionalization by tannic acid (MNPs@TA). The surface properties and molecular structures of the immobilized arylsulfatase (MNPs@TA@ARS) were examined by scanning electron microscopy and Fourier transform infrared spectroscopy. Enzymatic characterization showed that MNPs@TA@ARS exhibited shifted optimal temperature and pH with deviated apparent K(m) and V(max) compared to its free counterpart. The immobilized arylsulfatase demonstrated improved thermal and pH stability and enhanced storage stability with modest reusability. In addition, MNPs@TA@ARS displayed enhanced tolerance to various inhibitors and detergents. The utilization of the immobilized arylsulfatase for agar desulfation brought the treated agar with improved quality. |
format | Online Article Text |
id | pubmed-8441490 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-84414902021-09-15 Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement Zhang, Chenghao Jiang, Zedong Li, Hebin Ni, Hui Zheng, Mingjing Li, Qingbiao Zhu, Yanbing Food Sci Nutr Original Research The presence of sulfate groups in agar compromises the agar quality by affecting the crosslinking during gelling process. Some arylsulfatases can catalyze the hydrolysis of sulfate bonds in agar to improve the agar quality. Immobilized arylsulfatases prove beneficial advantages for their industrial applications. Here, a previously characterized mutant arylsulfatase K253H/H260L was immobilized on the synthesized magnetic Fe(3)O(4) nanoparticles after functionalization by tannic acid (MNPs@TA). The surface properties and molecular structures of the immobilized arylsulfatase (MNPs@TA@ARS) were examined by scanning electron microscopy and Fourier transform infrared spectroscopy. Enzymatic characterization showed that MNPs@TA@ARS exhibited shifted optimal temperature and pH with deviated apparent K(m) and V(max) compared to its free counterpart. The immobilized arylsulfatase demonstrated improved thermal and pH stability and enhanced storage stability with modest reusability. In addition, MNPs@TA@ARS displayed enhanced tolerance to various inhibitors and detergents. The utilization of the immobilized arylsulfatase for agar desulfation brought the treated agar with improved quality. John Wiley and Sons Inc. 2021-07-07 /pmc/articles/PMC8441490/ /pubmed/34532007 http://dx.doi.org/10.1002/fsn3.2446 Text en © 2021 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Zhang, Chenghao Jiang, Zedong Li, Hebin Ni, Hui Zheng, Mingjing Li, Qingbiao Zhu, Yanbing Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title | Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title_full | Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title_fullStr | Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title_full_unstemmed | Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title_short | Preparation of immobilized arylsulfatase on magnetic Fe(3)O(4) nanoparticles and its application for agar quality improvement |
title_sort | preparation of immobilized arylsulfatase on magnetic fe(3)o(4) nanoparticles and its application for agar quality improvement |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8441490/ https://www.ncbi.nlm.nih.gov/pubmed/34532007 http://dx.doi.org/10.1002/fsn3.2446 |
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