کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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599464 | 1454281 | 2014 | 6 صفحه PDF | دانلود رایگان |
• The double layer mixed matrix membranes (MMMs) were used to purify protein.
• The double layer MMMs consist of an active support and separating layer.
• The active support comprise of hydroxyapatite inside polyether sulfone matrix.
• The MMMs were characterized concerning permeability and adsorption capacity.
• The MMMs show purification of protein via both diffusion as well as adsorption.
This work proposed a novel approach for protein purification by using double layer mixed matrix membranes (MMMs). The double layer MMMs consisting of an active support and separating layer were prepared by co-casting two polymer solutions onto a glass plate. The active support layer consisted of nano hydroxyapatite (HAP) particles embedded in macroporous polyether sulfone (PES) and the separating layer was particle free PES membrane. The influence of separating layer with different PES content on membrane morphology was studied. The double layer MMMs were further characterized concerning permeability and adsorption capacity. The double layer MMMs showed purification of protein via diffusion as well as adsorption. The bovine serum albumin (BSA) was used as a model protein. The properties and structures of double layer MMMs prepared by immersion phase separation process were characterized by pure water flux, BSA adsorption and scanning electron microscopy (SEM).
A novel double layer MMMs combining diffusion and adsorption of BSA retention solutes in one step were prepared. The double layer MMMs consisted of an active support and separating layer. The active support layer consisted of nano hydroxyapatite (HAP) particles embedded in macroporous polyether sulfone (PES) and the separating layer was particle free PES membrane. The MMMs kept good filtration, adsorption and desorption properties.Figure optionsDownload as PowerPoint slide
Journal: Colloids and Surfaces B: Biointerfaces - Volume 123, 1 November 2014, Pages 33–38