Preparation and Characterization of Polyacrylonitrile Membranes Modified With Polyelectrolyte Deposition for Separating Similar Sized Proteins
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Date
2012
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier Ltd.
Open Access Color
BRONZE
Green Open Access
Yes
OpenAIRE Downloads
0
OpenAIRE Views
3
Publicly Funded
No
Abstract
One of the challenges faced by ultrafiltration membranes is to separate proteins with a small difference in their molecular weights. Recently, some researchers tried to overcome this problem by using charged membranes. This study examined the use of layer by layer deposition of polyelectrolytes on the chemically-modified polyacyronitrile membrane to increase the selectivity of the ultrafiltration. The membranes were prepared by wet-phase inversion technique and polyethylenimine (PEI) and alginate (ALG) were chosen as cationic and anionic polyelectrolytes for the modification of the surfaces. Sieving coefficient data were obtained with myoglobin and lysozyme as model proteins. The influences of solution pH, ionic strengths of the protein and polyelectrolyte solution and the number of polyelectrolyte bilayers on both selectivity and throughput were investigated. The highest selectivity and throughput were achieved with the 1-bilayer PEI-ALG coated polyacrylonitrile (PAN) membrane. Increasing the number of coating bilayers or the ionic strength of the protein solution or adding salt into the polyelectrolyte coating solution decreased both the maximum selectivity and throughput of the modified membranes.
Description
Keywords
Lysozyme, Myoglobin, Polyacrylonitrile, Polyelectrolytes, Ultrafiltration, Myoglobin, Lysozyme, Ultrafiltration, Polyacrylonitrile, Polyelectrolytes
Fields of Science
02 engineering and technology, 0210 nano-technology, 01 natural sciences, 0104 chemical sciences
Citation
Yaşar Mahlıçlı, F., Alsoy Altınkaya, S. and Yürekli, Y. (2012). Preparation and characterization of polyacrylonitrile membranes modified with polyelectrolyte deposition for separating similar sized proteins. Journal of Membrane Science, 415-416, 383-390. doi:10.1016/j.memsci.2012.05.028
WoS Q
Q1
Scopus Q
Q1

OpenCitations Citation Count
28
Source
Journal of Membrane Science
Volume
415-416
Issue
Start Page
383
End Page
390
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Citations
CrossRef : 19
Scopus : 33
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Mendeley Readers : 32
SCOPUS™ Citations
33
checked on Apr 27, 2026
Web of Science™ Citations
30
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Page Views
747
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Downloads
490
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