Interfacial microenvironment for lipase immobilization: Regulating the heterogeneity of graphene oxide
Article
Article Title | Interfacial microenvironment for lipase immobilization: Regulating the heterogeneity of graphene oxide |
---|---|
ERA Journal ID | 3854 |
Article Category | Article |
Authors | Zhuang, Wei (Author), Quan, Xuebo (Author), Wang, Zhenfu (Author), Zhou, Wenfeng (Author), Yang, Pengpeng (Author), Ge, Lei (Author), Villacorta Hernandez, Byron (Author), Wu, Jinglan (Author), Li, Ming (Author), Zhou, Jian (Author), Zhu, Chenjie (Author) and Ying, Hanjie (Author) |
Journal Title | Chemical Engineering Journal |
Journal Citation | 394, pp. 1-13 |
Article Number | 125038 |
Number of Pages | 13 |
Year | 2020 |
Publisher | Elsevier |
Place of Publication | Netherlands |
ISSN | 1385-8947 |
1873-3212 | |
Digital Object Identifier (DOI) | https://doi.org/10.1016/j.cej.2020.125038 |
Web Address (URL) | https://www.sciencedirect.com/science/article/abs/pii/S1385894720310305 |
Abstract | Compared to the traditional chemical reduction method, a green and efficient strategy was successfully applied to regulate the surface heterogeneity of graphene oxide (GO). In this work, different kinds of amino acids were used to reduce and modify GO. The reduction and adsorption disparities of amino acids contributed to the difference of structural heterogeneity in terms of density, thermal tolerance and disorder of the oxygen-containing groups of GO. The modification also resulted in discrepancies in surface properties of the GO samples, such as hydrophobicity and surface charge. The functionalized GO was employed as a carrier for the immobilization of lipase from Thermomyces lanuginosus (lipase TL). The storage stability, the temperature and pH sensitivity of the immobilized biocatalysts and the free lipase TL were studied. Lipase immobilized on functionalized GO demonstrates superior enzymatic loading and relative activity compared to GO, with a maximum increase of 70% and 47%, respectively. The relative activity of lipase immobilized on functionalized GO was 19.21 times more than that of commercial immobilized lipase TLIM. Through molecular dynamics simulations we concluded that the increase in the relative activity of lipase TL is mainly related to its adsorption orientation and slight conformational change. Thus, our research offered a green and effective strategy to regulate the heterogeneity of nanomaterials for a suitable microenvironment to enhance the performance of immobilized lipase. |
Keywords | Graphene oxide; Lipase; Interfacial heterogeneity; Enzymatic immobilization; Microenvironment |
ANZSRC Field of Research 2020 | 340399. Macromolecular and materials chemistry not elsewhere classified |
400408. Reaction engineering (excl. nuclear reactions) | |
Byline Affiliations | Nanjing Tech University, China |
South China University of Technology, China | |
Centre for Future Materials | |
University of Queensland | |
Institution of Origin | University of Southern Queensland |
https://research.usq.edu.au/item/q5v83/interfacial-microenvironment-for-lipase-immobilization-regulating-the-heterogeneity-of-graphene-oxide
130
total views9
total downloads2
views this month0
downloads this month