Supplementary Materials
Alginate dialdehyde meets nylon membrane: A versatile platform for facile and green fabrication of membrane adsorbers
M. Kamran Khan, a, b Jianquan Luo, a, b* Zhaoshuai Wang, a, b Rashid Khan, a, b Xiangrong Chen, a
Yinhua Wan a,b*
a State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of
Sciences, Beijing 100190, PR Chinab University of Chinese Academy of Sciences, Beijing 100049, PR China
*Corresponding authors: E-mail: [email protected] (J. Luo); [email protected] (Y. Wan)
Tel/Fax: +86-10-62650673
Alginate dialdehyde (ADA) Molecular weight
Molecular Weight of ADA was determined by using HPLC-GEC. A 30 cm x 0.75 cm TSK-G4000
PW column (Toyo Soda, Tokyo, Japan) preceded by a 2- µm filter (Rheodyne, CA) was equipped
with a Hitachi pump (Model L-6000), a precision injection valve (Rheodyne, 50 µL sample
loading) and a differential refractometer (R401 Waters Associates, France) connected to a
computer for sample detection. Dextran standards and glucose were injected at a
concentration of 1 mg/mL to establish the selectivity curve of the column. Injection volume was
40 µL for all analyses.
The calculated weight of the ADA was 150-200 KDa.
Membrane characterization by ATR-FTIR
The FTIR spectrum of pristine nylon, ADA-nylon, S-ADA-nylon (CEX), Me-affinity, His-affinity and
Pep-affinity are shown in Fig. S1. The peak at 1529 cm-1 corresponds to amides while the peak
at 1625 cm-1 shows carboxyl and carbonyl groups. Successful ADA coating was confirmed by the
appearance of new aldehyde and hydroxyl peaks around 1725 cm-1 and 3400 cm-1 respectively,
along with an increase in the carboxyl peak for ADA-nylon membrane. The disappearance of
aldehyde peak in the remaining scans confirms the successful immobilization of Sulphonic acid,
Electronic Supplementary Material (ESI) for Journal of Materials Chemistry B.This journal is © The Royal Society of Chemistry 2018
Histidine, Peptide and Me-affinity ligands via a Schiff’s base reaction. In the scan for S-ADA-
nylon membrane, the two new peaks for sulphonic groups at 1150 cm-1 and 1346 cm-1
confirmed the successful fabrication of S-ADA-nylon adsorber. The appearance of a broad peak
in Me-affinity nylon scan around 1180 cm- is for the chelated carboxylic groups. Successful
immobilization of histidine and peptide was confirmed by the increase in NH peak due to the
presence of NH groups in histidine and peptide.
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Pristine Nylon
C=OAldehyde
O-H
N-H
C=O ADA-Nylon
N-H
C=O
O-H
Sulphonic Peaks
Abs
orba
nce
CEX adsorber C=O
O-H
N-H Me-affinity adsorber
Chelated Carboxylic
N-HC=O
O-H
Wavenumbers (cm-1)
Pep-affinity adsorber N-HC=O
O-H
His-affinity adsorber
Figure S1. ATR-FTIR spectrum for pristine nylon, ADA-nylon, S-ADA nylon (CEX), Me-Affinity, His-
affinity and Pep-affinity adsorbers.
Figure S2. SEM Surface images of pristine nylon (a), CEX (b), Me-affinity (c), His-affinity (d) and
Pep-affinity (e) adsorbers.
Figure S3(a) . EDS spectra of pristine nylon membrane
Surface Scan
Figure S3 (b). SEM/EDS elemental mapping analysis (5000 x) of pristine nylon membrane, including surface topography, and individual elemental distribution map of C, O and N.
Figure S4 (a). EDS Spectra of ADA-Nylon membrane
Surface
Figure S4 (b). SEM/EDS elemental mapping analysis (5000 x) of ADA-Nylon membrane, including surface topography, and individual elemental distribution map of C, O and N.
Figure S5 (a). EDS Spectra of CEX membrane adsorber
Surface
Figure S5 (b). SEM/EDS elemental mapping analysis (5000 x) of CEX membrane adsorber, including surface topography, and individual elemental distribution map of C, O, N and S.
Figure S6 (a). EDS Spectra of Me-affinity membrane adsorber
ScanSurface Scan
Figure S6 (b). SEM/EDS elemental mapping analysis (5000 x) of Me-affinity membrane adsorber, including surface topography, and individual elemental distribution map of C, O, N and Cu.
Figure S7 (a). EDS Spectra of His-affinity membrane adsorber
Surface Scan
Figure S7 (b). SEM/EDS elemental mapping analysis (5000 x) of His-affinity membrane adsorber, including surface topography, and individual elemental distribution map of C, O and N.
Figure S8 (a). EDS Spectra of Pep-affinity membrane adsorber
ScanSurface Scan
Figure S8 (b). SEM/EDS elemental mapping analysis (5000 x) of Pep-affinity membrane adsorber, including surface topography (a), and individual elemental distribution map of C, O and N.
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Elution fraction
Time (min)
Flow through
UV a
bsor
banc
e (AU
)
HSAIgG
Feed IgG/HSA
Figure S9. High performance gel filtration chromatography results of feed, flow-through and
elution fractions obtained by pristine nylon membrane.
Figure S10. AKTA binding and elution chromatograms for the purification of IgG from IgG/HSA mixture by CEX (a), Me-affinity (b), His-affinity (c) and Pep-affinity (d) membrane adsorbers.
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ance
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Figure S11. AKTA chromatogram for IgG purification from Human serum by CEX (a) and Pep-affinity (b) adsorbers. The shoulder in the elution peak was due to the absorbance by KSCN.