Surface functionalization of graphene oxide by amino acids for Thermomyces lanuginosus lipase adsorption
Article
Article Title | Surface functionalization of graphene oxide by amino acids for Thermomyces lanuginosus lipase adsorption |
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ERA Journal ID | 1454 |
Article Category | Article |
Authors | Zhou, Wenfeng (Author), Zhuang, Wei (Author), Ge, Lei (Author), Wang, Zhenfu (Author), Wu, Jinglan (Author), Niu, Huanqing (Author), Liu, Dong (Author), Zhu, Chenjie (Author), Chen, Yong (Author) and Ying, Hanjie (Author) |
Journal Title | Journal of Colloid and Interface Science |
Journal Citation | 546, pp. 211-220 |
Number of Pages | 10 |
Year | 2019 |
Publisher | Elsevier |
Place of Publication | United States |
ISSN | 0021-9797 |
1095-7103 | |
Digital Object Identifier (DOI) | https://doi.org/10.1016/j.jcis.2019.03.066 |
Web Address (URL) | https://www.sciencedirect.com/science/article/pii/S0021979719303625 |
Abstract | Graphene oxide (GO) with oxygen containing functional groups can be selectively modified by small biomolecules to achieve heterogeneous surface properties. To achieve a hyper-enzymatic activity, the surface functionality of GO should be tailored to the orientation adsorption of the Thermomyces lanuginosus (TL) lipase, and the active center can be covered by a relatively hydrophobic helical lid for protection. In this work, amino acids were used to interact with GO through reduction reaction, hydrophobic forces, electrostatic forces, or hydrogen bonding to alter the surface hydrophobicity and charge density. Characterization of the structure and surface properties confirmed that the GO samples decorated with phenylalanine (Phe) and glutamic acid (Glu) exhibited superior hydrophobicity than other modifications, whereas tryptophan (Trp) and cysteine (Cys) provided weaker reduction effects on GO. Moreover, the zeta potential of the samples modified by amino acids of lysine (Lys) and arginine (Arg) is higher than other modified samples. The adsorption amount of lipase on Glu-GO reached 172 mg/g and the relative enzymatic activity reached up to 200%. The thermodynamic data and the Freundlich isotherm model fitting showed that the lipase adsorption process on modified samples was spontaneous, endothermic and entropy increase. |
Keywords | Lipase adsorption, Graphene oxide, Surface modification, Freundlich isotherm model, Amino acids |
ANZSRC Field of Research 2020 | 340305. Physical properties of materials |
340399. Macromolecular and materials chemistry not elsewhere classified | |
400408. Reaction engineering (excl. nuclear reactions) | |
Public Notes | Files associated with this item cannot be displayed due to copyright restrictions. |
Byline Affiliations | Nanjing Tech University, China |
Centre for Future Materials | |
Institution of Origin | University of Southern Queensland |
https://research.usq.edu.au/item/q5315/surface-functionalization-of-graphene-oxide-by-amino-acids-for-thermomyces-lanuginosus-lipase-adsorption
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