| Nome: | Descrição: | Tamanho: | Formato: | |
|---|---|---|---|---|
| 7.64 MB | Adobe PDF |
Autores
Orientador(es)
Resumo(s)
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.
Descrição
Palavras-chave
Whey protein hydrolysate Bioactive peptides Electrodialysis Ultrafiltration membrane Peptide fractionation β-lactoglobulin
