Xf. Zeng et E. Ruckenstein, CROSS-LINKED MACROPOROUS CHITOSAN ANION-EXCHANGE MEMBRANES FOR PROTEIN SEPARATIONS, Journal of membrane science, 148(2), 1998, pp. 195-205
Macroporous chitosan membranes with controlled pore sizes and good mec
hanical properties were prepared and crosslinked with ethylene glycol
diglycidyl ether to increase their chemical stability. Because of thei
r amine groups, they can serve as anion-exchangers (with an ion-exchan
ge capacity as high as 0.83 meq/g dry cross-linked membrane) and can b
e employed for protein separations in the ion-exchange mode. At pH<7,
their surface is positively charged. and they can adsorb proteins with
a pI<6 at appropriate pHs. Five proteins, namely ovalbumin (pI=4.6),
human serum albumin (pI=4.8), soybean trypsin inhibitor (pI=4.5), lyso
zyme (pI=11) and cytochrome C (pI=10.6) were selected as model protein
s to investigate their adsorption on the chitosan membranes. Relativel
y high dynamic capacities were achieved at a flow rate of 2 ml/min, na
mely 11.6, 19 and 20.8 mg/ml membrane for human serum albumin, ovalbum
in and soybean trypsin inhibitor, respectively. These proteins could b
e efficiently recovered (91-98%) from the membranes using a 1 N NaCl i
n 0.02 N sodium phosphate solution (pH 6) as eluant. Protein separatio
ns were performed from binary mixtures (ovalbumin-lysozyme, human seru
m albumin-cytochrome C, and soybean trypsin inhibitor-cytochrome C), a
nd high purity products (similar to 99%) obtained in a single pass. Th
ese membranes showed high stability and reproducibility. (C) 1998 Else
vier Science B.V. All rights reserved.