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Separation Of Bioactive Peptides From Whey Hydrolysate Using Electrodialysis With Ultrafiltration Membrane: A Pilot-Scale Study And Investigation On Process Parameters

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A tryptic hydrolysis of whey protein isolate has generated 19 peptides from β-lactoglobulin source, out of 27 peptide sequences detected under HPLC-MS. Amongst 19 peptides, 12 were detected as anionic peptides and 5 as cationic peptides. The aim of this work was to investigate the process parameters for fractionating bioactive peptides from protein hydrolysate by pilot-scale electrodialysis with ultrafiltration membrane (EDUF) unit. Preliminary tests were performed to evaluate process parameters. A pressure-flow relation was studied for establishing no transmembrane pressure. Protein hydrolysate was fractionated during 60 minutes by EDUF on a pilot-scale EUR6 module. Under a constant pH of 6 and electric field strength of 0.7 V/cm, peptide migration rates of 0.57 ± 0.25!!/!!ℎ and 0.29 ± 0.09!!/!!ℎ were achieved in anionic and cationic peptides recovery compartments respectively. An experiment was also further investigated under two electric field conditions: pulsed electric field (PEF) and reverse polarity (RP) to observe the effect on migration rate and selectivity. Total migration rates were found to be 0.51 ± 0.05 and 0.38 ± 0.15 !/!!ℎ under PEF and RP conditions, respectively. An application of PEF and RP were able to separate selectively few of peptides. Peptide migration rate and selective separation of peptides found to be strongly depended on electric field strength and pressure/flow rate in each compartment. It is the low electric field and relatively higher pressure that hinders the simultaneous separation of anionic and cationic peptides in their respective compartment. To our knowledge, it was the first attempt to study separation of bioactive peptides from whey protein isolate in a pilot scale EDUF module.

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Whey protein hydrolysate Bioactive peptides Electrodialysis Ultrafiltration membrane Peptide fractionation β-lactoglobulin

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