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Tailoring mesoporous-silica nanoparticles for robust immobilization of lipase and biocatalysis
The rational design of nano-carriers is critical for modem enzyme immobilization for advanced biocatalysis. Herein, we report the synthesis of octadecylalkyl- modified mesoporous-silica nanoparticles （C18-MSNs） with a high C18 content （-19 wt.%） and tunable pore sizes （1.6--13 nm）. It is demonstrate...
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| Published in: | Nano research 2017-02, Vol.10 (2), p.605-617 |
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| Main Authors: | , , , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c409t-90c9fcc947259a5b32972e41685db2a07d7b77158ff096e5b726c6e229fee3533 |
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| cites | cdi_FETCH-LOGICAL-c409t-90c9fcc947259a5b32972e41685db2a07d7b77158ff096e5b726c6e229fee3533 |
| container_end_page | 617 |
| container_issue | 2 |
| container_start_page | 605 |
| container_title | Nano research |
| container_volume | 10 |
| creator | Kalantari, Mohammad Yu, Meihua Yang, Yannan Strounina, Ekaterina Gu, Zhengying Huang, Xiaodan Zhang, Jun Song, Hao Yu, Chengzhong |
| description | The rational design of nano-carriers is critical for modem enzyme immobilization for advanced biocatalysis. Herein, we report the synthesis of octadecylalkyl- modified mesoporous-silica nanoparticles （C18-MSNs） with a high C18 content （-19 wt.%） and tunable pore sizes （1.6--13 nm）. It is demonstrated that the increased hydrophobic content and a tailored pore size （slightly larger than the size of lipase） are responsible for the high performance of immobilized lipase. The optimized C18-MSNs exhibit a loading capacity of 711 mg/g and a specific activity 5.23 times higher than that of the free enzyme. Additionally, 93% of the initial activity is retained after reuse five times, which is better than the best performance reported to date. Our findings pave the way for the robust immobilization of lipase for biocatalytic applications. |
| doi_str_mv | 10.1007/s12274-016-1320-6 |
| format | article |
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Herein, we report the synthesis of octadecylalkyl- modified mesoporous-silica nanoparticles （C18-MSNs） with a high C18 content （-19 wt.%） and tunable pore sizes （1.6--13 nm）. It is demonstrated that the increased hydrophobic content and a tailored pore size （slightly larger than the size of lipase） are responsible for the high performance of immobilized lipase. The optimized C18-MSNs exhibit a loading capacity of 711 mg/g and a specific activity 5.23 times higher than that of the free enzyme. Additionally, 93% of the initial activity is retained after reuse five times, which is better than the best performance reported to date. Our findings pave the way for the robust immobilization of lipase for biocatalytic applications.</description><identifier>ISSN: 1998-0124</identifier><identifier>EISSN: 1998-0000</identifier><identifier>DOI: 10.1007/s12274-016-1320-6</identifier><language>eng</language><publisher>Beijing: Tsinghua University Press</publisher><subject>Atomic/Molecular Structure and Spectra ; Biomedicine ; Biotechnology ; Catalysis ; Chemistry and Materials Science ; Condensed Matter Physics ; Enzymes ; Hydrophobicity ; Immobilization ; Lipase ; Materials Science ; Nanoparticles ; Nanostructure ; Nanotechnology ; Pore size ; Porosity ; Research Article ; Robustness ; Silica ; Silicon dioxide</subject><ispartof>Nano research, 2017-02, Vol.10 (2), p.605-617</ispartof><rights>Tsinghua University Press and Springer-Verlag Berlin Heidelberg 2017</rights><rights>Nano Research is a copyright of Springer, (2017). 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| identifier | ISSN: 1998-0124 |
| ispartof | Nano research, 2017-02, Vol.10 (2), p.605-617 |
| issn | 1998-0124 1998-0000 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1884128103 |
| source | Springer Link |
| subjects | Atomic/Molecular Structure and Spectra Biomedicine Biotechnology Catalysis Chemistry and Materials Science Condensed Matter Physics Enzymes Hydrophobicity Immobilization Lipase Materials Science Nanoparticles Nanostructure Nanotechnology Pore size Porosity Research Article Robustness Silica Silicon dioxide |
| title | Tailoring mesoporous-silica nanoparticles for robust immobilization of lipase and biocatalysis |
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