Abstract
Separation and purification processes of neutraceuticals, such as bioactive peptides, are usually done in a multistep process that sometimes requires a final chromatographic step using expensive resins. Activated carbon is a promising economic alternative for the resins. We report here on the application of a hydrophobic interaction on a chromatographic column packed with particles of activated carbon to isolate a lactotripeptide from a crude hydrolysate. Consecutive adsorptive–desorptive cycles were used until exhaustion of the column. Liquid chromatography–mass spectrometry results showed an enrichment of the lactotripeptide isoleucine–proline–proline with a yield of up to 80% in the third cycle and a twofold increase in purity to up to 35%. Some guidelines are given for the competitive exhaustion of the adsorbent for process optimization in order to obtain higher purity and yield.
Original language | English |
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Pages (from-to) | 255-262 |
Journal | Food and Bioproducts Processing |
Volume | 94 |
DOIs | |
Publication status | Published - 2015 |
Keywords
- hydrophobic interaction chromatography
- high fischer ratio
- enzyme-inhibitory properties
- pore-size distribution
- competitive adsorption
- protein hydrolysate
- binding-capacity
- peptide mixture
- antioxidant
- water