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Applied and Environmental Microbiology, September 2003, p. 5297-5305, Vol. 69, No. 9
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.9.5297-5305.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Angiotensin I-Converting-Enzyme-Inhibitory and Antibacterial Peptides from Lactobacillus helveticus PR4 Proteinase-Hydrolyzed Caseins of Milk from Six Species

F. Minervini,1,2 F. Algaron,3 C. G. Rizzello,1 P. F. Fox,4 V. Monnet,3 and M. Gobbetti1*

Dipartimento di Protezione delle Piante e Microbiologia Applicata, Facoltà di Agraria, Università degli Studi di Bari,1 Dipartimento di Scienze degli Alimenti, Università degli Studi di Perugia, Italy,2 Unité de Biochimie et Structure des Protéines, INRA, 78352 Jouy-en-Josas, France,3 Department of Food and Nutritional Sciences, University College, Cork, Ireland4

Received 26 February 2003/ Accepted 3 July 2003

Sodium caseinates prepared from bovine, sheep, goat, pig, buffalo or human milk were hydrolyzed by a partially purified proteinase of Lactobacillus helveticus PR4. Peptides in each hydrolysate were fractionated by reversed-phase fast-protein liquid chromatography. The fractions which showed the highest angiotensin I-converting-enzyme (ACE)-inhibitory or antibacterial activity were sequenced by mass spectrum and Edman degradation analyses. Various ACE-inhibitory peptides were found in the hydrolysates: the bovine {alpha}S1-casein ({alpha}S1-CN) 24-47 fragment (f24-47), f169-193, and ß-CN f58-76; ovine {alpha}S1-CN f1-6 and {alpha}S2-CN f182-185 and f186-188; caprine ß-CN f58-65 and {alpha}S2-CN f182-187; buffalo ß-CN f58-66; and a mixture of three tripeptides originating from human ß-CN. A mixture of peptides with a C-terminal sequence, Pro-Gly-Pro, was found in the most active fraction of the pig sodium caseinate hydrolysate. The highest ACE-inhibitory activity of some peptides corresponded to the concentration of the ACE inhibitor (S)-N-(1-[ethoxycarbonyl]-3-phenylpropyl)-ala-pro maleate (enalapril) of 49.253 µg/ml (100 µmol/liter). Several of the above sequences had features in common with other ACE-inhibitory peptides reported in the literature. The 50% inhibitory concentration (IC50) of some of the crude peptide fractions was very low (16 to 100 µg/ml). Some identified peptides were chemically synthesized, and the ACE-inhibitory activity and IC50s were confirmed. An antibacterial peptide corresponding to ß-CN f184-210 was identified in human sodium caseinate hydrolysate. It showed a very large spectrum of inhibition against gram-positive and -negative bacteria, including species of potential clinical interest, such as Enterococcus faecium, Bacillus megaterium, Escherichia coli, Listeria innocua, Salmonella spp., Yersinia enterocolitica, and Staphylococcus aureus. The MIC for E. coli F19 was ca. 50 µg/ml. Once generated, the bioactive peptides were resistant to further degradation by proteinase of L. helveticus PR4 or by trypsin and chymotrypsin.

* Corresponding author. Mailing address: Dipartimento di Protezione delle Piante e Microbiologia Applicata, Facoltà di Agraria, Università degli Studi di Bari, Via G. Amendola 165/a, 70125 Bari, Italy. Phone: 39 080 5442949. Fax: 39 080 5442911. E-mail: gobbetti{at}agr.uniba.it.

Applied and Environmental Microbiology, September 2003, p. 5297-5305, Vol. 69, No. 9
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.9.5297-5305.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lamothe, S., Robitaille, G., St-Gelais, D., Britten, M. (2007). Short Communication: Extraction of {beta}-Casein from Goat Milk. J DAIRY SCI 90: 5380-5382 [Abstract] [Full Text]  
  • Hayes, M., Stanton, C., Slattery, H., O'Sullivan, O., Hill, C., Fitzgerald, G. F., Ross, R. P. (2007). Casein Fermentate of Lactobacillus animalis DPC6134 Contains a Range of Novel Propeptide Angiotensin-Converting Enzyme Inhibitors. Appl. Environ. Microbiol. 73: 4658-4667 [Abstract] [Full Text]  
  • Rizzello, C. G., Losito, I., Gobbetti, M., Carbonara, T., De Bari, M. D., Zambonin, P. G. (2005). Antibacterial Activities of Peptides from the Water-Soluble Extracts of Italian Cheese Varieties. J DAIRY SCI 88: 2348-2360 [Abstract] [Full Text]  


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