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Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme
Immobilized enzymes are a significant technological approach to retain enzyme activity and reduce enzyme catalytic cost. In this work, trypsin-incorporated Zn(3)(PO(4))(2) hybrid nanoflowers were prepared via mild precipitation and coordination reactions. The controllable preparation of hybrid nanof...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9569851/ https://www.ncbi.nlm.nih.gov/pubmed/36233153 http://dx.doi.org/10.3390/ijms231911853 |
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author | Wang, Zichao Liu, Pei Fang, Ziyi Jiang, He |
author_facet | Wang, Zichao Liu, Pei Fang, Ziyi Jiang, He |
author_sort | Wang, Zichao |
collection | PubMed |
description | Immobilized enzymes are a significant technological approach to retain enzyme activity and reduce enzyme catalytic cost. In this work, trypsin-incorporated Zn(3)(PO(4))(2) hybrid nanoflowers were prepared via mild precipitation and coordination reactions. The controllable preparation of hybrid nanoflowers was achieved by systematically investigating the effects of the raw-material ratio, material concentration and reaction temperature on product morphology and physicochemical properties. The enzyme content of hybrid nanoflowers was about 6.5%, and the maximum specific surface area reached 68.35 m(2)/g. The hybrid nanoflowers exhibit excellent catalytic activity and environmental tolerance compared to free trypsin, which was attributed to the orderly accumulation of nanosheets and proper anchoring formation. Further, the enzyme activity retention rate was still higher than 80% after 12 repeated uses. Therefore, trypsin/Zn(3)(PO(4))(2) hybrid nanoflowers—which combine functionalities of excellent heat resistance, storage stability and reusability—exhibit potential industrial application prospects. |
format | Online Article Text |
id | pubmed-9569851 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95698512022-10-17 Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme Wang, Zichao Liu, Pei Fang, Ziyi Jiang, He Int J Mol Sci Article Immobilized enzymes are a significant technological approach to retain enzyme activity and reduce enzyme catalytic cost. In this work, trypsin-incorporated Zn(3)(PO(4))(2) hybrid nanoflowers were prepared via mild precipitation and coordination reactions. The controllable preparation of hybrid nanoflowers was achieved by systematically investigating the effects of the raw-material ratio, material concentration and reaction temperature on product morphology and physicochemical properties. The enzyme content of hybrid nanoflowers was about 6.5%, and the maximum specific surface area reached 68.35 m(2)/g. The hybrid nanoflowers exhibit excellent catalytic activity and environmental tolerance compared to free trypsin, which was attributed to the orderly accumulation of nanosheets and proper anchoring formation. Further, the enzyme activity retention rate was still higher than 80% after 12 repeated uses. Therefore, trypsin/Zn(3)(PO(4))(2) hybrid nanoflowers—which combine functionalities of excellent heat resistance, storage stability and reusability—exhibit potential industrial application prospects. MDPI 2022-10-06 /pmc/articles/PMC9569851/ /pubmed/36233153 http://dx.doi.org/10.3390/ijms231911853 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Zichao Liu, Pei Fang, Ziyi Jiang, He Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title | Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title_full | Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title_fullStr | Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title_full_unstemmed | Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title_short | Trypsin/Zn(3)(PO(4))(2) Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
title_sort | trypsin/zn(3)(po(4))(2) hybrid nanoflowers: controlled synthesis and excellent performance as an immobilized enzyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9569851/ https://www.ncbi.nlm.nih.gov/pubmed/36233153 http://dx.doi.org/10.3390/ijms231911853 |
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