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Toward controlled geometric structure and surface property heterogeneities of TiO2 for lipase immobilization
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  • Wenfeng Zhou,
  • Xiaohong Zhou,
  • Wei Zhuang,
  • Rijia Lin,
  • Ye Zhao,
  • Lei Ge,
  • Ming Li,
  • Jinglan Wu,
  • Pengpeng Yang,
  • Hongman Zhang,
  • Chenjie Zhu,
  • Hanjie Ying
Wenfeng Zhou
Nanjing Tech University
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Xiaohong Zhou
Nanjing Tech University
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Wei Zhuang
Nanjing Tech University
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Rijia Lin
The University of Queensland
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Ye Zhao
Zhengzhou University
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Lei Ge
University of Southern Queensland
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Ming Li
Nanjing Tech University
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Jinglan Wu
Nanjing Tech University
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Pengpeng Yang
Nanjing Tech University
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Hongman Zhang
Nanjing Tech University
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Chenjie Zhu
Nanjing Tech University
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Hanjie Ying
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Abstract

Immobilized enzymes as biocatalysts are expected to solve issues of pollution and economic inefficiency in industrial catalysis. In order to obtain an immobilized enzyme with high activity and stability, the design of substrate geometric structure and surface properties is desirable. Here, TiO2 with controlled pore size and surface properties was designed and synthesized for lipase immobilization, resulting in an efficient biocatalyst. The activity of TiO2 immobilized lipase is improved with the increasing pore size of TiO2 from 10 to 100 nm. Compared to geometric structure impact, regulation of surface properties plays a greater role on the immobilization of lipase on TiO2. Among them, the relative activity of ethenyl triethoxy silane (ETS) modified TiO2 immobilized lipase is as high as 365.85 % over the pristine lipase. This research provides experimental evidence for studying the adsorption of enzyme molecules on the supports under the synergistic effect of geometric structure and surface properties.