Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> 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<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> hybrid nanoflowers were prepared via mild precipitation and coord...
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MDPI AG
2022-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/19/11853 |
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| author | Zichao Wang Pei Liu Ziyi Fang He Jiang |
| author_facet | Zichao Wang Pei Liu Ziyi Fang He Jiang |
| author_sort | Zichao Wang |
| collection | DOAJ |
| description | Immobilized enzymes are a significant technological approach to retain enzyme activity and reduce enzyme catalytic cost. In this work, trypsin-incorporated Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> 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<sup>2</sup>/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<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> hybrid nanoflowers—which combine functionalities of excellent heat resistance, storage stability and reusability—exhibit potential industrial application prospects. |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T21:37:05Z |
| publishDate | 2022-10-01 |
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| spelling | doaj.art-34fd92a622964da99c39eaafbf16d0982023-11-23T20:40:22ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-10-0123191185310.3390/ijms231911853Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized EnzymeZichao Wang0Pei Liu1Ziyi Fang2He Jiang3The Key Laboratory of Space Applied Physics and Chemistry, Ministry of Education, Shaanxi Key Laboratory of Macromolecular Science and Technology, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi’an 710072, ChinaThe Key Laboratory of Space Applied Physics and Chemistry, Ministry of Education, Shaanxi Key Laboratory of Macromolecular Science and Technology, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi’an 710072, ChinaThe Key Laboratory of Space Applied Physics and Chemistry, Ministry of Education, Shaanxi Key Laboratory of Macromolecular Science and Technology, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi’an 710072, ChinaThe Key Laboratory of Space Applied Physics and Chemistry, Ministry of Education, Shaanxi Key Laboratory of Macromolecular Science and Technology, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, Xi’an 710072, ChinaImmobilized enzymes are a significant technological approach to retain enzyme activity and reduce enzyme catalytic cost. In this work, trypsin-incorporated Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> 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<sup>2</sup>/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<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> hybrid nanoflowers—which combine functionalities of excellent heat resistance, storage stability and reusability—exhibit potential industrial application prospects.https://www.mdpi.com/1422-0067/23/19/11853hybrid materialstrypsinnanoflowerscontrolled synthesiscatalytic performance |
| spellingShingle | Zichao Wang Pei Liu Ziyi Fang He Jiang Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme International Journal of Molecular Sciences hybrid materials trypsin nanoflowers controlled synthesis catalytic performance |
| title | Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
| title_full | Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
| title_fullStr | Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
| title_full_unstemmed | Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
| title_short | Trypsin/Zn<sub>3</sub>(PO<sub>4</sub>)<sub>2</sub> Hybrid Nanoflowers: Controlled Synthesis and Excellent Performance as an Immobilized Enzyme |
| title_sort | trypsin zn sub 3 sub po sub 4 sub sub 2 sub hybrid nanoflowers controlled synthesis and excellent performance as an immobilized enzyme |
| topic | hybrid materials trypsin nanoflowers controlled synthesis catalytic performance |
| url | https://www.mdpi.com/1422-0067/23/19/11853 |
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