Presence of free amino acids in protein hydrolysate during electroseparation of peptides: Impact on system efficiency and membrane physicochemical properties
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Presence of free amino acids in protein hydrolysate during electroseparation of peptides : Impact on system efficiency and membrane physicochemical properties. / Suwal, Shyam; Roblet, Cyril; Amiot, Jean; Bazinet, Laurent.
In: Separation and Purification Technology, Vol. 147, 2015, p. 227-236.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Presence of free amino acids in protein hydrolysate during electroseparation of peptides
T2 - Impact on system efficiency and membrane physicochemical properties
AU - Suwal, Shyam
AU - Roblet, Cyril
AU - Amiot, Jean
AU - Bazinet, Laurent
PY - 2015
Y1 - 2015
N2 - Abstract Membranes, more particularly ion-exchange membranes (IEMs), are vulnerable to fouling by peptides and amino acids present in protein hydrolysate. In this context, IEM and ultrafiltration membranes (UFMs) staked in an electrodialysis with filtration membrane (EDFM) system were characterized during and after 6 successive peptide fractionations. The peptide concentration in the recovery compartment decreased by more than 22% and 32% for fifth and sixth batches, respectively. In addition, analysis of total nitrogen content of used membranes and FTIR confirmed that AEM and both cation-exchange membranes (CEMs) were fouled by peptides and/or free amino acids. Consequently, their electrical conductivity, IEC and water content decreased. In addition to the fouling, the cathode (diluate) side of AEM, where the dissociation of water molecules occurs, was deteriorated radically, possibly due to chemical reactions with OH− ions produced. Consequently, the surface roughness of both IEMs was found to increase considerably. The IEM fouling noticed in the present study was never observed before in an EDFM treatment. This fouling would be mainly due to the presence of amino acids residues (100% free) in the SCBH, and able to migrate through the AEM (Phe) and the CEM (Arg and Lys).
AB - Abstract Membranes, more particularly ion-exchange membranes (IEMs), are vulnerable to fouling by peptides and amino acids present in protein hydrolysate. In this context, IEM and ultrafiltration membranes (UFMs) staked in an electrodialysis with filtration membrane (EDFM) system were characterized during and after 6 successive peptide fractionations. The peptide concentration in the recovery compartment decreased by more than 22% and 32% for fifth and sixth batches, respectively. In addition, analysis of total nitrogen content of used membranes and FTIR confirmed that AEM and both cation-exchange membranes (CEMs) were fouled by peptides and/or free amino acids. Consequently, their electrical conductivity, IEC and water content decreased. In addition to the fouling, the cathode (diluate) side of AEM, where the dissociation of water molecules occurs, was deteriorated radically, possibly due to chemical reactions with OH− ions produced. Consequently, the surface roughness of both IEMs was found to increase considerably. The IEM fouling noticed in the present study was never observed before in an EDFM treatment. This fouling would be mainly due to the presence of amino acids residues (100% free) in the SCBH, and able to migrate through the AEM (Phe) and the CEM (Arg and Lys).
KW - Characterization
KW - Electrodialysis with ultrafiltration membrane
KW - Ion exchange membrane
KW - Membrane fouling
KW - Peptide separation
U2 - 10.1016/j.seppur.2015.04.014
DO - 10.1016/j.seppur.2015.04.014
M3 - Journal article
VL - 147
SP - 227
EP - 236
JO - Gas Separation and Purification
JF - Gas Separation and Purification
SN - 1383-5866
ER -
ID: 204114306