Internal membrane fouling by proteins during microfiltration
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 electro...
| Үндсэн зохиолчид: | , , , , , |
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| Формат: | Journal Article |
| Хэл сонгох: | English |
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2022
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| Нөхцлүүд: | |
| Онлайн хандалт: | https://hdl.handle.net/10356/160466 |
| _version_ | 1826125853039263744 |
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| author | Lay, Huang Teik Yeow, Rique Jie En Ma, Yunqiao Zydney, Andrew L. Wang, Rong Chew, Jia Wei |
| author2 | School of Chemical and Biomedical Engineering |
| author_facet | School of Chemical and Biomedical Engineering Lay, Huang Teik Yeow, Rique Jie En Ma, Yunqiao Zydney, Andrew L. Wang, Rong Chew, Jia Wei |
| author_sort | Lay, Huang Teik |
| collection | NTU |
| description | 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 (α) and pore constriction (β), 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 (α) 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 μm layer (i.e., 4.5 μm 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. |
| first_indexed | 2024-10-01T06:43:10Z |
| format | Journal Article |
| id | ntu-10356/160466 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:43:10Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-10356/1604662022-07-25T01:01:47Z Internal membrane fouling by proteins during microfiltration Lay, Huang Teik Yeow, Rique Jie En Ma, Yunqiao Zydney, Andrew L. Wang, Rong Chew, Jia Wei School of Chemical and Biomedical Engineering Interdisciplinary Graduate School (IGS) School of Civil and Environmental Engineering Singapore Membrane Technology Centre Nanyang Environment and Water Research Institute Engineering::Chemical engineering Membrane Fouling Surface Charge 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 (α) and pore constriction (β), 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 (α) 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 μm layer (i.e., 4.5 μm 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. Agency for Science, Technology and Research (A*STAR) Economic Development Board (EDB) Ministry of Education (MOE) We acknowledge funding from the Singapore GSK (GlaxoSmithKline)-EDB (Economic Development Board) Trust Fund, A*STAR (Singapore) Advanced Manufacturing and Engineering (AME) under its Pharma Innovation Programme Singapore (PIPS) program (A20B3a0070), A*STAR (Singapore) Advanced Manufacturing and Engineering (AME) under its Individual Research Grant (IRG) program (A2083c0049), the Singapore Ministry of Education Academic Research Fund Tier 1 Grant (2019-T1-002-065; RG100/19), and the Singapore Ministry of Education Tier 2 Academic Research Fund (MOE-MOET2EP10120-0001). 2022-07-25T01:01:47Z 2022-07-25T01:01:47Z 2021 Journal Article Lay, H. T., Yeow, R. J. E., Ma, Y., Zydney, A. L., Wang, R. & Chew, J. W. (2021). Internal membrane fouling by proteins during microfiltration. Journal of Membrane Science, 637, 119589-. https://dx.doi.org/10.1016/j.memsci.2021.119589 0376-7388 https://hdl.handle.net/10356/160466 10.1016/j.memsci.2021.119589 2-s2.0-85109686195 637 119589 en A20B3a0070 A2083c0049 2019-T1-002-065; RG100/19 MOE-MOET2EP10120-0001 Journal of Membrane Science © 2021 Elsevier B.V. All rights reserved. |
| spellingShingle | Engineering::Chemical engineering Membrane Fouling Surface Charge Lay, Huang Teik Yeow, Rique Jie En Ma, Yunqiao Zydney, Andrew L. Wang, Rong Chew, Jia Wei Internal membrane fouling by proteins during microfiltration |
| title | Internal membrane fouling by proteins during microfiltration |
| title_full | Internal membrane fouling by proteins during microfiltration |
| title_fullStr | Internal membrane fouling by proteins during microfiltration |
| title_full_unstemmed | Internal membrane fouling by proteins during microfiltration |
| title_short | Internal membrane fouling by proteins during microfiltration |
| title_sort | internal membrane fouling by proteins during microfiltration |
| topic | Engineering::Chemical engineering Membrane Fouling Surface Charge |
| url | https://hdl.handle.net/10356/160466 |
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