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Applied and Environmental Microbiology, July 2007, p. 4658-4667, Vol. 73, No. 14
0099-2240/07/$08.00+0     doi:10.1128/AEM.00096-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Casein Fermentate of Lactobacillus animalis DPC6134 Contains a Range of Novel Propeptide Angiotensin-Converting Enzyme Inhibitors{triangledown}

M. Hayes,1,2 C. Stanton,1,3 H. Slattery,1 O. O'Sullivan,1 C. Hill,2,3 G. F. Fitzgerald,2,3 and R. P. Ross1,3*

Teagasc Biotechnology Centre, Moorepark Food Research, Fermoy, County Cork, Ireland,1 Department of Microbiology, University College, Cork, Ireland,2 Alimentary Pharmabiotic Centre, Cork, Ireland3

Received 15 January 2007/ Accepted 23 April 2007

This work evaluated the angiotensin-converting-enzyme (ACE)-inhibitory activities of a bovine sodium caseinate fermentate generated using the proteolytic capabilities of the porcine small intestinal isolate Lactobacillus animalis DPC6134 (NCIMB deposit 41355). The crude 10-kDa L. animalis DPC6134 fermentate exhibited ACE-inhibitory activity of 85.51% (±15%) and had a 50% inhibitory concentration (IC50) of 0.8 mg protein/ml compared to captopril, which had an IC50 value of 0.005 mg/ml. Fractionation of the crude L. animalis DPC6134 fermentate by membrane filtration and reversed-phase high-performance liquid chromatography (HPLC) generated three bioactive fractions from a total of 72 fractions. Fractions 10, 19, and 43 displayed ACE-inhibitory activity percentages of 67.53 (±15), 83.71 (±19), and 42.36 (±11), respectively, where ACE inhibition was determined with 80 µl of the fractions with protein concentrations of 0.5 mg/ml. HPLC and mass spectrometry analysis identified 25 distinct peptide sequences derived from {alpha}-, ß-, and {kappa}-caseins. In silico predictions, based on the C-terminal tetrapeptide sequences, suggested that peptide NIPPLTQTPVVVPPFIQ, corresponding to ß-casein f(73-89); peptide IGSENSEKTTMP, corresponding to {alpha}s1-casein f(201212); peptide SQSKVLPVPQ, corresponding to ß-casein f(166-175); peptide MPFPKYPVEP, corresponding to ß-casein f(124133); and peptide EPVLGPVRGPFP, corresponding to ß-casein f(210-221), contained ACE-inhibitory activities. These peptides were chosen for chemical synthesis to confirm the ACE-inhibitory activity of the fractions. Chemically synthesized peptides displayed IC50 values in the range of 92 µM to 790 µM. Additionally, a simulated gastrointestinal digestion confirmed that the ACE-inhibitory 10-kDa L. animalis DPC6134 fermentation was resistant to a cocktail of digestive enzymes found in the gastrointestinal tract.

* Corresponding author. Mailing address: Teagasc, Biotechnology Centre, Moorepark, Fermoy, County Cork, Ireland. Phone: 353 (0) 2542229. Fax: 353 (0) 2542340. E-mail: paul.ross{at}teagasc.ie

{triangledown} Published ahead of print on 4 May 2007.

Applied and Environmental Microbiology, July 2007, p. 4658-4667, Vol. 73, No. 14
0099-2240/07/$08.00+0     doi:10.1128/AEM.00096-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gagnaire, V., Jardin, J., Jan, G., Lortal, S. (2009). Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances. J DAIRY SCI 92: 811-825 [Abstract] [Full Text]  


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