期刊
JOURNAL OF MEMBRANE SCIENCE
卷 637, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.memsci.2021.119589
关键词
Membrane fouling; Surface charge; In situ monitoring; Fouling model; Microfiltration
资金
- Singapore GSK (GlaxoSmithKline) - EDB (Economic Development Board) Trust Fund
- A*STAR (Singapore) Advanced Manufacturing and Engineering (AME) [A20B3a0070, A2083c0049]
- Singapore Ministry of Education Academic Research Fund Tier 1 Grant [2019T1002065, RG100/19]
- Singapore Ministry of Educa-tion Tier 2 Academic Research Fund [MOE-MOET2EP10120-0001]
This study investigated the external and internal membrane fouling caused by three proteins with different net charges. Results showed that lysozyme had the most severe impact on flux decline, followed by BSA. Various analysis methods revealed different characteristics of protein fouling on the membrane surface.
The current study aimed to understand both external and internal membrane fouling by three proteins with different net charges, namely, negatively charged pepsin and bovine serum albumin (BSA), as well as positively charged lysozyme. Polycarbonate track-etched (PCTE) membranes were used. Per electrostatic attraction, the flux decline was the worst for lysozyme, which is attributed by the fouling model to the greatest pore blockage (alpha) and pore constriction (beta), and by field-emission scanning electron microscope (FESEM) and optical coherence tomography (OCT) to the most extensive external fouling. Between pepsin and BSA, BSA gave worse flux decline despite its more negative net charge. The fouling model indicates that BSA gave greater pore blockage (alpha) and denser internal cake (Rc/Rm), while the quartz crystal microbalance with dissipation (QCM-D) indicates a rigid cake structure. Notably, despite monotonic flux decline with filtration, the OCT fouling voxel trends show significant fluctuations, which has not been reported before and thus signify the unique behavior of protein foulants in straight-through pores. Specifically, the trends below and above the -4.5 mu m layer (i.e., 4.5 mu m below the feed-membrane interface) are perfectly opposite, indicating the non-uniform protein deposits slipping downwards in the membrane pores as filtration progressed. The dynamic movements of the protein cakes unveiled here warrant more understanding in future studies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据