Key Laboratory for Green Chemical Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
Bioresour Technol. 2011 Jan;102(2):647-51. doi: 10.1016/j.biortech.2010.08.030. Epub 2010 Aug 10.
Constructing anti-fouling and self-cleaning membrane surfaces based on covalent attachment of trypsin on poly(methacrylic acid)-graft-polyethersulfone (PMAA-g-PES) membrane was reported. The carboxylic acid groups enriched on asymmetric PMAA-g-PES membrane surface were activated with 1-ethyl-(3-3-dimethylaminopropyl)-carbodiimide hydrochloride (EDC)/N-hydroxysuccinimide (NHS) and employed as chemical anchors for the conjugation with amino groups of trypsin. Activity assays showed that such chemically immobilized trypsin was much more active and stable than that of the physically adsorbed counterpart. Trypsin covalently attached on membrane surface could substantially resist protein fouling in dynamic flow process. The considerable enhancement of protein solution permeation flux was observed as a consequence of rapid enzymatic degradation of protein deposited onto membrane surface. The permeation flux of the membrane could be recovered upon simple hydraulic flush after protein filtration, suggesting superior self-cleaning property. After multi-cycle BSA filtration over 15-day period, the active self-cleaning membrane maintained more than 95.0% of its initial flux.
据报道，通过在聚（甲基丙烯酸）-接枝-聚醚砜（PMAA-g-PES）膜上共价附着胰蛋白酶，构建了具有抗污染和自清洁功能的膜表面。不对称 PMAA-g-PES 膜表面上富集的羧酸基团用 1-乙基-（3-3-二甲基氨基丙基）碳化二亚胺盐酸盐（EDC）/N-羟基琥珀酰亚胺（NHS）活化，并用作与胰蛋白酶氨基的化学连接点。活性测定表明，这种化学固定化的胰蛋白酶比物理吸附的胰蛋白酶活性和稳定性更高。固定在膜表面上的胰蛋白酶可以在动态流动过程中显著抵抗蛋白质污染。由于沉积在膜表面上的蛋白质迅速被酶降解，因此观察到蛋白质溶液渗透通量的显著提高。在蛋白质过滤后，只需简单的水力冲洗即可恢复膜的渗透通量，表明其具有优异的自清洁性能。在经过 15 天的多周期 BSA 过滤后，活性自清洁膜保持了初始通量的 95.0%以上。
