دورية أكاديمية
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Supreme Catalytic Properties of Enzyme Nanoparticles Based on Ferritin Self-Assembly.

التفاصيل البيبلوغرافية
العنوان: Supreme Catalytic Properties of Enzyme Nanoparticles Based on Ferritin Self-Assembly.
المؤلفون: Chen Q; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Guangdong Laboratory for Lingnan Modern Agriculture, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Key Laboratory of Zoonosis of Ministry of Agriculture and Rural Affairs, South China Agricultural University, Guangzhou, Guangdong 510642, China., Men D; State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China., Sun T; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China., Zhang Y; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China., Yuan Q; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China., Hu T; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China., Hu Z; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China., Wu J; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Guangdong Laboratory for Lingnan Modern Agriculture, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Key Laboratory of Zoonosis of Ministry of Agriculture and Rural Affairs, South China Agricultural University, Guangzhou, Guangdong 510642, China., Deng Y; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Guangdong Laboratory for Lingnan Modern Agriculture, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Key Laboratory of Zoonosis of Ministry of Agriculture and Rural Affairs, South China Agricultural University, Guangzhou, Guangdong 510642, China., Zhang XE; National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China., Wen J; Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Guangdong Laboratory for Lingnan Modern Agriculture, South China Agricultural University, Guangzhou, Guangdong 510642, China.; Key Laboratory of Zoonosis of Ministry of Agriculture and Rural Affairs, South China Agricultural University, Guangzhou, Guangdong 510642, China.
المصدر: ACS applied bio materials [ACS Appl Bio Mater] 2020 Oct 19; Vol. 3 (10), pp. 7158-7167. Date of Electronic Publication: 2020 Sep 23.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: ACS Publications Country of Publication: United States NLM ID: 101729147 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2576-6422 (Electronic) Linking ISSN: 25766422 NLM ISO Abbreviation: ACS Appl Bio Mater Subsets: PubMed not MEDLINE; MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : ACS Publications, [2018]-
مستخلص: In this study, we aimed to address if enzymes self-assembled on the biological nanosphere matrix would have some nanoscale effects and then improve the catalytic ability and other characteristics especially for the resistance to adverse conditions. Initially, we evaluated two different forms of ferritins, DNA-binding protein from starved cells (Dps) and recombinant heavy chain of human ferritin (rHF), fused with methyl parathion hydrolase (MPH) to be self-assembled as the dodecamer and 24-mer enzyme nanoparticles (enzyme-NPs), Dps-MPH and MPH-rHF. Both self-assembled enzyme-NPs showed superior catalytic activity and k cat drastically increased, but MPH-rHF showed better performance than Dps-MPH. Next, Escherichia coli alkaline phosphatase (EAP) and the canonical mutant EAP(D101S) were chosen to confirm if rHF-based self-assembly generally improves the catalysis of enzymes with the different catalytic abilities. Additionally, restoration of the enzyme native forms on the rHF shell by increasing the flexibility of the polylinker between the catalytic units and the nanoscaffold further improved the catalytic activities of enzyme-NPs. Some of the nanoparticles exhibited better residual activities under extreme conditions. Conclusively, the enzyme-NPs based on rHF self-assembly provided an effective strategy for enzyme engineering.
فهرسة مساهمة: Keywords: catalytic activity; enzyme nanoparticle; nanocarrier; recombinant heavy chain of human ferritin; self-assembly
تواريخ الأحداث: Date Created: 20220112 Latest Revision: 20220210
رمز التحديث: 20240829
DOI: 10.1021/acsabm.0c00961
PMID: 35019374
قاعدة البيانات: MEDLINE
الوصف
تدمد:2576-6422
DOI:10.1021/acsabm.0c00961