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Proposing sequences for peptides derived from whey fermentation with potential bioactive sites
M A Belem1, B F Gibbs, B H Lee
1Department of Food Science and Agricultural Chemistry, McGill University, Ste.-Anne-de-Bellevue, PQ, Canada.
Abstract:
In fed-batch fermentation by Kluyveromyces marxianus var. marxianus, whey-soluble proteins were converted into oligopeptides. To assess whether bioactive peptides could be produced during whey fermentation, K. marxianus was cultured in batch in deproteinized media containing 5 or 15% (wt/vol) dehydrated whey for 20 h and then was in fed-batch mode for 50 h. After harvesting the biomass (25,000 x g, 15 min), at 6-h intervals, the wort was analyzed to determine protein consumption and oligopeptide production by HPLC. The proteins in the wort showed an oscillatory degradation with a constant increase in the production of oligopeptides. Four major peaks were collected and were analyzed by API mass spectroscopy. Sequences of fermented peptides were compared with sequences of known bioactive peptides. On the basis of their molecular weights, two amino acid sequences were proposed. The presence of sites containing the peptide sequence of beta-lactorphin (YLLF) suggests that these oligopeptides may have antihypertensive properties.
Insights
Kluyveromyces marxianus fermentation converts whey proteins into bioactive oligopeptides. Analysis suggests these peptides, including beta-lactorphin, may possess antihypertensive properties, offering potential health benefits.
Area of Science:
- Biotechnology
- Food Science
- Biochemistry
Background:
- Whey proteins are a rich source of peptides.
- Kluyveromyces marxianus is a yeast with known protein-degrading capabilities.
- Bioactive peptides derived from food proteins hold potential health benefits.
Purpose of the Study:
- To investigate the production of bioactive peptides from whey proteins using Kluyveromyces marxianus.
- To analyze the peptide sequences generated during fermentation for potential bioactivity.
- To assess the antihypertensive potential of fermentation-derived oligopeptides.
Main Methods:
- Fed-batch fermentation of Kluyveromyces marxianus in whey-based media.
- High-performance liquid chromatography (HPLC) for protein and oligopeptide analysis.
- API mass spectrometry for peptide sequencing and identification.
Main Results:
- Whey proteins were effectively converted into oligopeptides during fermentation.
- Oscillatory protein degradation and continuous oligopeptide production were observed.
- Two potential bioactive peptide sequences were proposed, including beta-lactorphin (YLLF).
Conclusions:
- Kluyveromyces marxianus fermentation is a viable method for producing oligopeptides from whey.
- The identified peptides, particularly beta-lactorphin, suggest potential antihypertensive properties.
- This study opens avenues for developing functional foods and nutraceuticals from whey protein.