Site-directed immobilization of enzymes on nanoparticles using self-assembly systems
Copyright © 2024. Published by Elsevier Ltd..
Enzyme immobilization is an effective method for improving the stability and reusability. However, linking at random sites on the enzyme results in low catalytic efficiency due to blockage of the active site or conformational changes. Therefore, controlling the orientation of enzymes on the carrier has been developed. Here, the site-specific mutation and the SpyTag/SpyCatcher systems were used to prepare a site-directed immobilized enzyme. The thermal stability of the immobilized enzyme was better than that of the free enzyme, and ≥80 % of the catalytic activity was retained after 30 days of storage. Furthermore, the Michaelis constant (Km) and the turnover number (kcat) of the immobilized enzyme were 5.23-fold lower and 6.11-fold higher than those of the free enzyme, respectively, which appeared to be related to changes in secondary structure after immobilization. These findings provide a new and effective option for enzyme-directed immobilization.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:397 |
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| Enthalten in: |
Bioresource technology - 397(2024) vom: 27. März, Seite 130505 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Zhou, Haili [VerfasserIn] |
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| Links: |
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| Themen: |
Enzymes, Immobilized |
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| Anmerkungen: |
Date Completed 14.03.2024 Date Revised 14.03.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.biortech.2024.130505 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM369133803 |
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| 520 | |a Copyright © 2024. Published by Elsevier Ltd. | ||
| 520 | |a Enzyme immobilization is an effective method for improving the stability and reusability. However, linking at random sites on the enzyme results in low catalytic efficiency due to blockage of the active site or conformational changes. Therefore, controlling the orientation of enzymes on the carrier has been developed. Here, the site-specific mutation and the SpyTag/SpyCatcher systems were used to prepare a site-directed immobilized enzyme. The thermal stability of the immobilized enzyme was better than that of the free enzyme, and ≥80 % of the catalytic activity was retained after 30 days of storage. Furthermore, the Michaelis constant (Km) and the turnover number (kcat) of the immobilized enzyme were 5.23-fold lower and 6.11-fold higher than those of the free enzyme, respectively, which appeared to be related to changes in secondary structure after immobilization. These findings provide a new and effective option for enzyme-directed immobilization | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Glutamate decarboxylase | |
| 650 | 4 | |a Self-assembly | |
| 650 | 4 | |a Site-directed immobilization | |
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| 700 | 1 | |a Fang, Yuling |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Jing |e verfasserin |4 aut | |
| 700 | 1 | |a Xiong, Tao |e verfasserin |4 aut | |
| 700 | 1 | |a Peng, Fei |e verfasserin |4 aut | |
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