Toward controlled geometric structure and surface property heterogeneities of TiO2 for lipase immobilization
Article
Zhou, Wenfeng, Zhou, Xiaohong, Zhuang, Wei, Lin, Rijia, Zhao, Ye, Ge, Lei, Li, Ming, Wu, Jinglan, Yang, Pengpeng, Zhang, Hongman, Zhu, Chenjie and Ying, Hanjie. 2021. "Toward controlled geometric structure and surface property heterogeneities of TiO2 for lipase immobilization." Process Biochemistry. 110, pp. 118-128. https://doi.org/10.1016/j.procbio.2021.08.004
Article Title | Toward controlled geometric structure and surface property heterogeneities of TiO2 for lipase immobilization |
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ERA Journal ID | 35021 |
Article Category | Article |
Authors | Zhou, Wenfeng, Zhou, Xiaohong, Zhuang, Wei, Lin, Rijia, Zhao, Ye, Ge, Lei, Li, Ming, Wu, Jinglan, Yang, Pengpeng, Zhang, Hongman, Zhu, Chenjie and Ying, Hanjie |
Journal Title | Process Biochemistry |
Journal Citation | 110, pp. 118-128 |
Number of Pages | 11 |
Year | 2021 |
Publisher | Elsevier |
Place of Publication | United Kingdom |
ISSN | 1359-5113 |
1873-3298 | |
Digital Object Identifier (DOI) | https://doi.org/10.1016/j.procbio.2021.08.004 |
Web Address (URL) | https://www.sciencedirect.com/science/article/abs/pii/S1359511321002397 |
Abstract | To effectively immobilize an enzyme while maintaining its high activity and stability, the design of supports with controlled geometric structures and heterogeneous surface properties is desirable. Towards this goal, heterogeneous titanium dioxide (TiO2) surfaces with controlled pore sizes were synthesized in this study and used to efficiently immobilize lipase. The immobilized lipase activity increased by a factor of 1.31 with an increase in the TiO2 pore size from 11.46 to 21.14 nm. The highest protein loading of 15.52 mg/g was achieved in ethenyl triethoxy silane (ETS)-modified TiO2 (E-P25) after immobilizing the enzymes at 30 ℃, pH 7.33 for 3 h and using a protein concentration in solution of 0.176 mg/mL. Among the different surface functionalities, the highest activity yield of 428.04 % was accomplished by using TiO2 calcinated at 650 ℃ and modified by ETS as immobilization support. The immobilized enzymes showed excellent storage stability and retained almost 95 % of their activity after being stored at 4 ℃ for 8 weeks. This research provides experimental evidence that highlights the importance of studying of enzyme immobilization on the supports with synergistically designed geometric structures and surface chemical properties. |
Keywords | Coupling agents; Heterogeneities; Titanium dioxide ; Coupling agents ; Lipase immobilization |
Contains Sensitive Content | Does not contain sensitive content |
ANZSRC Field of Research 2020 | 340202. Crystallography |
Public Notes | The accessible file is the submitted version of the paper. Please refer to the URL for the published version. |
Byline Affiliations | Nanjing Tech University, China |
University of Queensland | |
Zhengzhou University, China | |
Centre for Future Materials |
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https://research.usq.edu.au/item/zq59z/toward-controlled-geometric-structure-and-surface-property-heterogeneities-of-tio2-for-lipase-immobilization
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