Electrodialytic separation of peptides from snow crab by-product hydrolysate: Effect of cell configuration on peptide selectivity and local electric field
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Electrodialytic separation of peptides from snow crab by-product hydrolysate : Effect of cell configuration on peptide selectivity and local electric field. / Suwal, Shyam; Roblet, Cyril; Doyen, Alain; Amiot, Jean; Beaulieu, Lucie; Legault, Jean; Bazinet, Laurent.
In: Separation and Purification Technology, Vol. 127, 2014, p. 29-38.Research output: Contribution to journal › Journal article › peer-review
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TY - JOUR
T1 - Electrodialytic separation of peptides from snow crab by-product hydrolysate
T2 - Effect of cell configuration on peptide selectivity and local electric field
AU - Suwal, Shyam
AU - Roblet, Cyril
AU - Doyen, Alain
AU - Amiot, Jean
AU - Beaulieu, Lucie
AU - Legault, Jean
AU - Bazinet, Laurent
PY - 2014
Y1 - 2014
N2 - Electrodialysis with ultrafiltration membrane (EDUF) has been successfully used to separate bioactive peptides from various food protein hydrolysates. Nevertheless, EDUF process was found to be affected by permeate and feed pHs, electric field strength and membrane materials, molecular weight cuf-off (MWCO) as well as surface area. In the present study, the effect of two EDUF cell configurations was examined on different electrodialytic parameters; first with one feed and two recovery compartments and second with two feed and one recovery compartments. The EDUF cell configurations had significant effect on peptide migration rate and selectivity such as amino acid composition and peptide molecular weight profiles of the permeate fractions obtained after 6 h of EDUF treatment. The configuration 1 led to the higher total peptide migration rate of 6.00 ± 0.12 g/(h m2) in comparison to 4.41 ± 0.20 g/(h m2) for configuration 2. However, in configuration 1, the local electric field in the hydrolysate compartment decreased linearly throughout EDUF process which limited peptide migration after about 2 h of EDUF treatment. Amino acid analysis of permeate fractions showed that anionic amino acids primarily Glu, Tau, Met and Phe were concentrated in both peptide recovery compartments of configuration 1, while cationic amino acids like Arg and Lys were mainly concentrated in peptide recovery compartment of configuration 2. © 2014 Elsevier B.V. All rights reserved.
AB - Electrodialysis with ultrafiltration membrane (EDUF) has been successfully used to separate bioactive peptides from various food protein hydrolysates. Nevertheless, EDUF process was found to be affected by permeate and feed pHs, electric field strength and membrane materials, molecular weight cuf-off (MWCO) as well as surface area. In the present study, the effect of two EDUF cell configurations was examined on different electrodialytic parameters; first with one feed and two recovery compartments and second with two feed and one recovery compartments. The EDUF cell configurations had significant effect on peptide migration rate and selectivity such as amino acid composition and peptide molecular weight profiles of the permeate fractions obtained after 6 h of EDUF treatment. The configuration 1 led to the higher total peptide migration rate of 6.00 ± 0.12 g/(h m2) in comparison to 4.41 ± 0.20 g/(h m2) for configuration 2. However, in configuration 1, the local electric field in the hydrolysate compartment decreased linearly throughout EDUF process which limited peptide migration after about 2 h of EDUF treatment. Amino acid analysis of permeate fractions showed that anionic amino acids primarily Glu, Tau, Met and Phe were concentrated in both peptide recovery compartments of configuration 1, while cationic amino acids like Arg and Lys were mainly concentrated in peptide recovery compartment of configuration 2. © 2014 Elsevier B.V. All rights reserved.
KW - Cell configuration
KW - Electrodialysis with ultrafiltration membrane
KW - Snow crab byproduct hydrolysate
U2 - 10.1016/j.seppur.2014.02.018
DO - 10.1016/j.seppur.2014.02.018
M3 - Journal article
VL - 127
SP - 29
EP - 38
JO - Gas Separation and Purification
JF - Gas Separation and Purification
SN - 1383-5866
ER -
ID: 204114284