Role of Protein Aggregation in Microfiltration

• Main Authors: Ching Hsuan-Tang, 湯景萱
• Other Authors: Daming-Wang
• Format: Others
• Language: zh-TW
• Published: 2001
• Online Access: http://ndltd.ncl.edu.tw/handle/81585349487187975888

碩士 === 國立臺灣大學 === 化學工程學研究所 === 89 === Fouling of protein in microfiltration is highly related to protein aggregation. Hence, experiments were performed with bovine serum albumin (BSA) and 0.2μm track-etched polycarbonate(PC) membranes to understand the role of protein aggregation in microfiltration. Surface structure of the fouled membranes was examined by using SEM and AFM. The composition of the fouling layer was analyzed by using FT-IR. It was found that the flux decline was initiated by the blocking of protein aggregates on membrane pores. Existence of protein aggregates in feed solution was confirmed by using light-scattering, light- diffraction, and HPLC. The fouling behavior can be divided into two stages. The initial fouling was due to the deposition of protein aggregates onto the membrane surface. And the resistance growth in long-term operation was originated from the compression of the deposition layer. The fouling behavior of cysteinyl-BSA and lysozyme was also studied and compared with that of BSA. The results demonstrated the importance of the free sulfhydryl group (-SH) in determining the compressibility of the aggregate layer. Besides, it was found that protein aggregates can be easily compressed on hydrophobic membranes because the protein can deform easily.