Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species

Applied and Environmental Microbiology

Volumn 69, Issue 9, 2003, Pages 5297-5305

  Minervini, F ^a   Algaron, F ^b   Rizzello, C G ^a   Fox, P F ^c   Monnet, V ^b   Gobbetti, M ^a  

^a UNIVERSITY OF BARI   (Italy)

^b CEMAGREF   (France)

^c UNIVERSITY COLLEGE CORK   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; ESCHERICHIA COLI; HYDROLYSIS; LIQUID CHROMATOGRAPHY; POLYPEPTIDES;

ANTIBACTERIAL PEPTIDES;

MICROBIOLOGY;

BACTERIAL ENZYME; CASEIN; CHYMOTRYPSIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENALAPRIL; PEPTIDE DERIVATIVE; PEPTIDE FRAGMENT; PROTEINASE; TRIPEPTIDE;

MICROBIOLOGY; MILK; PEPTIDE;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS MEGATERIUM; BACTERIAL STRAIN; BUFFALO; CATTLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG ACTIVITY; DRUG SYNTHESIS; ENTEROCOCCUS FAECIUM; ESCHERICHIA COLI; FAST PROTEIN LIQUID CHROMATOGRAPHY; GOAT; HUMAN; IC 50; LACTOBACILLUS HELVETICUS; LISTERIA INNOCUA; MASS SPECTROMETRY; MILK; NONHUMAN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SALMONELLA; SHEEP; SPECIES DIFFERENCE; STAPHYLOCOCCUS AUREUS; SWINE; YERSINIA ENTEROCOLITICA;

AMINO ACID SEQUENCE; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; ANTI-BACTERIAL AGENTS; BACILLUS MEGATERIUM; BUFFALOES; CASEINS; CATTLE; ENDOPEPTIDASES; ESCHERICHIA COLI; GOATS; HUMANS; HYDROLYSIS; LACTOBACILLUS; MICROBIAL SENSITIVITY TESTS; MILK; MILK, HUMAN; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; SPECIES SPECIFICITY;

BACILLUS MEGATERIUM; BACTERIA (MICROORGANISMS); BOS TAURUS; BOVINAE; BUBALUS; CAPRA; CAPRA HIRCUS; ENTEROCOCCUS; ENTEROCOCCUS FAECIUM; ESCHERICHIA COLI; LACTOBACILLUS; LACTOBACILLUS HELVETICUS; LISTERIA; LISTERIA INNOCUA; NEGIBACTERIA; OVIS; OVIS ARIES; POSIBACTERIA; SALMONELLA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS PHAGE 187; SUS SCROFA; YERSINIA; YERSINIA ENTEROCOLITICA;

EID: 0141816841     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.9.5297-5305.2003     Document Type: Article

References (47)

1. Aniansson, G., B. Andersson, R. Lindstedt, and C. Svanborg. 1990. Antiadhesive activity of human casein against Streptococcus termophilus and Haemophilus influenzae. Microb. Pathog. 8:315-323.
2. Barefoot, S. F., and T. R. Klaenhammer. 1983. Detection and activity of lactacin B, a bacteriocin produced by Lactobacillus acidophilus. Appl. Environ. Microbiol. 45:1808-1815.
3. Bechinger, B. 1997. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
4. Blondelle, S. E., and K. Lohner. 2000. Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55:74-87.
5. Bullen, J. J., H. J. Rogers, and L. Leigh. 1972. Iron binding proteins in milk and resistance to E. coli infections in infants. Brit. Med. J. 1:69-75.
6. Church, F. C., H. E. Swaisgood, D. H. Porter, and G. L. Catignani. 1983. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci. 66:1219-1227.
7. Clare, D. A., and H. E. Swaisgood. 2000. Bioactive milk peptides: a prospectus. J. Dairy Sci. 83:1187-1195.
8. Crow, V. L., R. Holland, and T. Coolbear. 1993. Comparison of subcellular fractionation methods for Lactococcus lactis ssp. lactis and Lactococcus lactis ssp. Cremoris. Int. Dairy J. 3:599-612.
9. Cushman, D. W., and H. S. Cheung. 1971. Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Biochem. Pharmacol. 20:1637-1648.
10. Devin, D. A., and R. E. W. Hancock. 2002. Cationic peptides: distribution and mechanism of resistance. Curr. Pharmacol. Design 8:703-714.
11. Dixon, M. 1953. The determination of enzyme inhibitor constants. Biochem. J. 55:170-171.
12. Dziuba, J., P. Mimkiewicz, and K. Plitnik. 1996. Chicken meat proteins as potential precursors of bioactive peptides. Pol. J. Food Nutr. Sci. 4:85-96.
13. Dziuba, J., P. Minkiewicz, D. Nalecz, and A. Iwaniak. 1999. Database of biologically active peptide sequences. Nahrung 43:190-195.
14. Epand, R. C., and H. J. Vogel. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462:11-28.
15. Ferreira, S. H., D. C. Bartet, and L. J. Greene. 1970. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry 9:2583-2593.
16. Fiat, A. M., and P. Jollès. 1989. Caseins of various origins and biologically active casein peptides and oligosaccharides: structural and physiological aspects. Mol. Cell. Biochem. 87:5-30.
17. FitzGerald, R. J., and H. Meisel. 2000. Milk protein-derived inhibitors of angiotensin-I-converting enzyme. Brit. J. Nutr. 1:S33-S37.
18. Ginger, M. R., and M. R. Grigor. 1999. Comparative aspects of milk caseins. Comp. Biochem. Physiol. B 124:133-145.
19. Gobbetti, M., P. Ferranti, E. Smacchi, F. Goffredi, and F. Addeo. 2000. Production of angiotensin-1 converting enzyme (ACE)-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Appl. Environ. Microbiol. 66:3898-3904.
20. Gobbetti, M., L. Stepaniak, M. De Angelis, A. Corsetti, and R. Di Cagno. 2002. Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing. Crit. Rev. Food Sci. Nutr. 42:223-239.
21. Hancock, R. E. W., and R. Leher. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88.
22. Kunji, E. R. S., I. Mierau, A. Hagting, B. Poolman, and N. Konings. 1996. The proteolytic system of lactic acid bacteria. Antonie Leeuwenhoek 70:187-221.
23. Lahov, E., and W. Regelson. 1996. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem. Toxicol. 34:131-145.
24. Liepke, C., H. D. Zucht, W. G. Forsmann, and L. Standker. 2001. Purification of novel peptide antibiotics from human milk. J. Chromatogr. 752:369-377.
25. Maruyama, S., K. Nakagomi, N. Tomizuka, and H. Suzuki. 1985. Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agric. Biol. Chem. 49:1405-1409.
26. Maruyama, S., H. Mitachi, H. Tanaka, N. Tomizuka, and H. Suzuki. 1987. Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein. Agric. Biol. Chem. 51:1581-1586.
27. Meisel, H. 1993. Casokinins as inhibitors of angiotensin-converting-enzyme, p. 153-159. In G. Sawatzki and B. Renner (ed.), New perspectives in infant nutrition. Thieme, Stuttgart, N.Y.
28. Meisel, H., and E. Schlimme. 1994. Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins), p. 27-33. In V. Brantl and H. Teschemacher (ed.), β-Casomorphins and related peptides: recent developments. Weinheim, VCH, New York, N.Y.
29. Meisel, H., S. Günther, D. Martin, and E. Schlimme. 1998. Apoptosis induced by modified ribonucleosides in human cell culture systems. FEBS Lett. 433:265-268.
30. Meisel, H. 2001. Bioactive peptides from milk proteins: a perspective for consumers and producers. Austr. J. Dairy Technol. 56:83-91.
31. Mullally, M. M., H. Meisel, and R. J. FitzGerald. 1996. Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity. Biol. Chem. Hoppe-Seyler 377:259-260.
32. Nakamura, Y., N. Yamamoto, K. Sakai, A. Okubo, S. Yamazaki, and T. Takano. 1995. Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk. J. Dairy Sci. 78:777-783.
33. Ng-Kwai Hang, K. F., and F. Grosclaude. 1992. Genetic polymorphisms of milk proteins, p. 405-455. In P. F. Fox (ed.), Advanced Dairy Chemistry. Elsevier, London, United Kingdom.
34. Petrillo, E. W., Jr., and M. A. Ondetti. 1982. Angiotensin converting enzyme inhibitors: medicinal chemistry and biological actions. Med. Res. Rev. 2:1-41.
35. s2-casein. Biochim. Biophys. Acta 1428:314-326.
36. Schanbacher, F. L., R. S. Talhouk, and F. A. Murray. 1997. Biology and origin of bioactive peptides in milk. Livest. Prod. Sci. 50:105-123.
37. Schillinger, U., and F. K. Lucke. 1989. Antibacterial activity of Lactobacillus sake isolated from meat. Appl. Environ. Microbiol. 55:1901-1906.
38. Shah, N. P. 2000. Effects of milk-derived bioactives: an overview. Brit. J. Nutr. 1:S3-S10.
39. Smacchi, E., and M. Gobbetti. 1998. Peptides from several Italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, Pseudomonas fluorescens ATCC 948 and to the angiotensin I-converting enzyme. Enzyme Microb. Technol. 22:687-694.
40. Stromqvist, M., P. Falk, S. Bergstrom, L. Hansson, B. Lonnerdal, S. Normark, and O. Hernell. 1995. Human milk κ-casein and inhibition of Helicobacter pylori adhesion to human gastric mucosa. J. Pediatr. Gastroenterol. Nutr. 21:288-296.
41. Tauzin, J., L Miclo, and J. L. Gaillard. 2002. Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine αs2-casein. FEBS Lett. 531:369-374.
42. Twinning, S. 1984. Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal. Biochem. 143:30-34.
43. Vermeirssen, V., J. Van Camp, and W. Verstraete. 2002. Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides. J. Biochem. Biophys. Methods 51:75-87.
44. Walker, J. R., J. R. Roth, and E. Altman. 2001. An in vivo study of novel bioactive peptides that inhibit the growth of Escherichia coli. J. Peptide Res. 58:380-388.
45. Yamamoto, N., A. Akino, and T. Takano. 1994. Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790. J. Dairy Sci. 77:917-922.
46. Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison. 1993. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
47. s2 derived peptide exhibits antibacterial activity. FEBS Lett. 372:185-188.