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Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides
Abstract
The aim of this study was to identify whey-derived peptides with angiotensin I-converting enzyme (ACE) inhibitory activity. The bovine whey proteins α-lactalbumin and β-lactoglobulin were hydrolysed with pepsin, trypsin, chymotrypsin, pancreatin, elastase or carboxypeptidase alone and in combination. The total hydrolysates were fractionated in a two step ultrafiltration process, first with a 30 kDa membrane and then with a 1 kDa membrane. Inhibition of ACE was analysed spectrophotometrically. The peptides were isolated by chromatography and identified by mass and sequencing analysis. The most potent inhibitory peptides were synthesized by the 9-fluorenylmethoxycarbonyl solid phase method. Inhibition of ACE was observed after hydrolysis with trypsin alone, and with an enzyme combination containing pepsin, trypsin and chymotrypsin. Whey protein digests gave a 50 % inhibition (IC 50) of ACE activity at concentration ranges within 345–1733 μg/ml. The IC 50 values for the 1–30 kDa fractions ranged from 485 to 1134 μg/ml and for the <1 kDa fraction from 109 to 837 mg/ml. Several ACE-inhibitory peptides were isolated from the hydrolysates by reversed-phase chromatography, and the potencies of the purified peptide fractions had IC 50 values of 77–1062 μ M. The ACE-inhibitory peptides identified were α-lactalbumin fractions (50–52), (99–108) and (104–108) and β-lactoglobulin fractions (22–25), (32–40), (81–83), (94–100), (106–111) and (142–146).
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Metadata
- Authors
- PIHLANTO-LEPPÄLÄ, A., KOSKINEN, P., PIILOLA, K., TUPASELA, T., & KORHONEN, H.
- Venue
- Journal of Dairy Research
- Publisher
- Cambridge University Press (CUP)
- Published
- 2000-02
- Volume
- 67
- Issue
- 1
- Pages
- 53-64
- ISSN
- 0022-0299 (ISSN-L)
- 1469-7629
- OpenAlex
- W2084256952
- Cited by
- 398
- References
- 0
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- closed
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