ANGIOTENSIN I-CONVERTING ENZYME (ACE) INHIBITORY PEPTIDES FROM WHEY FERMENTED BY LACTOBACILLUS SPECIES

Authors: AHN, J.E.¹; PARK, S.Y.¹; ATWAL, A.²; GIBBS, B.F.³; LEE, B.H.

Source: Journal of Food Biochemistry, Volume 33, Number 4, August 2009 , pp. 587-602(16)

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Abstract:

From 2% (w/w) whey powder in growth media, inhibitory peptides against angiotensin I-converting enzyme (ACE) were studied with nine Lactobacillus species. Lb. brevis, Lb. helveticus and Lb. paracasei were proved to be the most effective strains in liberating ACE inhibitory peptides from whey protein. The inhibition rates of these peptides against ACE ranging from 93.3 to 100%. Several distinct peaks were eluted when the whey proteins were fractionated on a Delta Pak C₁₈ column by reversed phase-high performance liquid chromatography (RP-HPLC). Among ACE inhibitory activities of 14 peptides purified by dialysis and by fractionation using RP-HPLC, two peptide fractions (H5 and H7) of Lb. helveticus showing IC₅₀ values of 5.3 and 7.8 were the most potent ACE inhibitors.

All of these peptides including some other peptides (H1 and B1), having strong inhibitory activities against ACE were pentapeptides positioning with Ala at their N-terminal and these petapeptides had mostly hydrophobic (Pro, Val and Leu) or aromatic (Phe) amino acids at the C-terminal. PRACTICAL APPLICATIONS

There is a significant amount of research and interest in developing and charactering the peptides that inhibit angiotensin I-converting enzyme (ACE) activity as these natural products may have a role in blood pressure control in man. This study revealed that the identification of peptides, mostly composed of pentapeptides following fermentation of whey protein in growth medium with different strains have the ACE inhibitory activities. These peptides may have antihypertensive effect as natural and safe nutraceutical/functional ingredients, though the exact potency of the pentapeptides isolated in this experiment has not been determined.

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1745-4514.2009.00239.x

Affiliations: 1: Food Science and Agricultural ChemistryMcGill UniversitySte-Anne-de-Bellevue, Quebec, H9X 3V9, Canada 2: Food R & D CentreAgriculture and Agri-Food CanadaSt. Hyacinthe, Quebec, J2S 8ES, Canada 3: Sheldon Biotechnology Center McGill University Montreal, Quebec, H3A 2B4, Canada

Publication date: 2009-08-01

ANGIOTENSIN I-CONVERTING ENZYME (ACE) INHIBITORY PEPTIDES FROM WHEY FERMENTED BY LACTOBACILLUS SPECIES

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