Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase
Article
Article Title | Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase |
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ERA Journal ID | 40638 |
Article Category | Article |
Authors | Zhang, Jihang (Author), Wang, Zhaoxin (Author), Zhuang, Wei (Author), Rabiee, Hesamoddin (Author), Zhu, Chenjie (Author), Deng, Jiawei (Author), Ge, Lei (Author) and Ying, Hanjie (Author) |
Journal Title | ACS Applied Materials and Interfaces |
Journal Citation | 14 (34), p. 39622−39636 |
Number of Pages | 15 |
Year | 2022 |
Publisher | American Chemical Society |
Place of Publication | United States |
ISSN | 1944-8244 |
1944-8252 | |
Digital Object Identifier (DOI) | https://doi.org/10.1021/acsami.2c11500 |
Web Address (URL) | https://pubs.acs.org/doi/10.1021/acsami.2c11500 |
Abstract | Graphene-based materials are widely used in the field of immobilized enzymes due to their easily tunable interfacial properties. We designed amphiphilic nanobiological interfaces between graphene oxide (GO) and lipase TL (Thermomyces lanuginosus) with tunable reduction degrees through molecular dynamics simulations and a facile chemical modulation, thus revealing the optimal interface for the interfacial activation of lipase TL and addressing the weakness of lipase TL, which exhibits weak catalytic activity due to an inconspicuous active site lid. It was demonstrated that the reduced graphene oxide (rGO) after 4 h of ascorbic acid reduction could boost the relative enzyme activity of lipase TL to reach 208%, which was 48% higher than the pristine GO and 120% higher than the rGO after 48 h of reduction. Moreover, TL–GO-4 h’s tolerance against heat, organic solvent, and long-term storage environment was higher than that of free TL. The drawbacks of strong hydrophobic nanomaterials on lipase production were explored in depth with the help of molecular dynamics simulations, which explained the mechanism of enzyme activity enhancement. We demonstrated that nanomaterials with certain hydrophilicity could facilitate the lipase to undergo interfacial activation and improve its stability and protein loading rate, displaying the potential of the extensive application. |
Keywords | immobilized lipase; reduced graphene oxide; molecular dynamics simulation; orientation; interfacial activation |
ANZSRC Field of Research 2020 | 400406. Powder and particle technology |
340303. Nanochemistry | |
340402. Biomolecular modelling and design | |
Public Notes | Files associated with this item cannot be displayed due to copyright restrictions. |
Byline Affiliations | Nanjing Tech University, China |
Zhengzhou University, China | |
Centre for Future Materials | |
Institution of Origin | University of Southern Queensland |
https://research.usq.edu.au/item/q7q3y/amphiphilic-nanointerface-inducing-the-interfacial-activation-for-lipase
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