Free Access
Issue
Lait
Volume 82, Number 6, November-December 2002
Page(s) 657 - 671
DOI https://doi.org/10.1051/lait:2002040

References

  1. Abo-Elnaga I.G., Plapp R., Peptidases of Lactobacillus casei and Lactobacillus plantarum, J. Basic Microbiol. 27 (1987) 123-130.
  2. Adda J., Gripon J.C., Vassal L., The chemistry of flavor and texture generation in cheese, Food Chem. 9 (1982) 115-129.
  3. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J., Basic local alignment search tool, J. Mol. Biol. 215 (1990) 403-410.
  4. Atlan D., Laloi P., Portalier R., X-prolyl-dipeptidyl-aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus: characterization of the enzyme and isolation of deficient mutants, Appl. Environ. Microbiol. 56 (1990) 2174-2179.
  5. Biswas I., Gruss A., Ehrlich S.D., Maguin E., High efficiency gene inactivation and replacement system for Gram positive bacteria, J. Bacteriol. 175 (1993) 3628-3635.
  6. Bockelmann W., Fobker M., Teuber M., Purification and characterisation of the X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus delbrueckii ssp. bulgaricus and Lactobacillus acidophilus, Int. Dairy J. 1 (1991) 51-66.
  7. Booth M., Fhaolain D., Jennings P.V., O'Cuinn G., Purification and characterization of a post-proline dipeptidyl aminopeptidase from Streptococcus cremoris AM2, J. Dairy Res. 57 (1990) 89-99.
  8. Casey M.G., Meyer J., Presence of X-prolyl-dipeptidyl-peptidase in lactic acid bacteria, J. Dairy Sci. 68 (1985) 3212-3215.
  9. Chich J.-F., Chapot-Chartier M.-P., Ribadeau-Dumas B., Gripon J.-C., Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis, FEBS Lett. 314 (1992) 139-142.
  10. Church F.C., Swaisgood H.E., Porter D.H., Catignani G.L., Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins, J. Dairy Sci. 66 (1983) 1219-1227.
  11. Cogan T.M., Hill C., Cheese Starter Cultures, in: Fox P.F. (Ed.), Cheese: Chemistry, Physics and Microbiology vol.1., Chapman & Hall, London, U.K., 1993, pp. 193-255.
  12. El Abboudi M., El Soda M., Pandian S., Simard R.E., Olson N.F., Purification of X-prolyl dipeptidyl aminopeptidase from Lactobacillus casei subspecies, Int. J. Food Microbiol. 15 (1992) 87-98.
  13. Escamilla-Hurtado M.L., Tomasini-Campocosio A., Valdes-Martinez S., Soriano-Santos J., Diacetyl formation by lactic bacteria, Rev. Latinoam. Microbiol. 38 (1996) 129-137.
  14. Ferretti J.J., McShan W.M., Ajdic D., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Quian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R., Complete genome sequence of an M1 strain of Streptococcus pyogenes, Proc. Natl. Acad. Sci. USA 98 (2001) 4658-4663.
  15. Fox P.F., Wallace J.M., Formation of flavour compounds, Adv. Appl. Microbiol. 45 (1997) 17-85.
  16. Fukasawa K.M., Harada M., Purification and properties of dipeptidyl peptidase IV from Streptococcus mitis ATCC 9811, Arch. Biochem. Biophys. 210 (1982) 230-237.
  17. Georgalaki M.D., Sarantinopoulos P., Ferreira E.S., De Vuyst L., Kalanzopoulos G., Tsakalidou E., Biochemical properties of Streptococcus macedonicus strains isolated from Greek Kasseri cheese, J. Appl. Microbiol. 88 (2000) 817-825.
  18. Gilliland S.E., Health and nutritional benefits from lactic acid bacteria, FEMS Microbiol. Rev. 7 (1990) 175-188.
  19. Habibi-Najafi M.B., Lee B.H., Purification and characterization of an X-prolyl-dipeptidyl aminopeptidase from Lactobacillus casei ssp. casei LLG, Appl. Microbiol. Biotechnol. 42 (1994) 280-286.
  20. Khalid N.M., Marth E.H., Purification and characterization of prolyl dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ 32, Appl. Environ. Microbiol. 56 (1990) 381-388.
  21. Kiefer-Partsch B., Bockelmann W., Geis A., Teuber M., Purification of an X-prolyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. cremoris, Appl. Microbiol. Biotechnol. 31 (1989) 75-78.
  22. Kilpper-Baelz R., Fischer G., Schleifer K.N., Nucleic acid hybridization of group N and group D streptococci, Curr. Microbiol. 7 (1982) 245-250.
  23. Kunji E.R.S., Mierau I., Hagting A., Poolman B., Konings W., The proteolytic systems of lactic acid bacteria, Antonie Leeuwenhoek 70 (1996) 187-221.
  24. Laemmli U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
  25. Law B.A., Kolstadt J., Proteolytic systems in lactic acid bacteria, Antonie Leeuwenhoek 49 (1983) 225-245.
  26. Leenhouts K.J., Kok J., Venema G., Cambell-like integration of heterologous plasmid DNA into the chromosome of Lactococcus lactis subsp. lactis, Appl. Environ. Microbiol. 55 (1989) 394-400.
  27. Leenhouts K.J., Kok J., Venema G., Stability of integrated plasmids in the chromosome of Lactococcus lactis, Appl. Environ. Microbiol. 56 (1990) 2726-2735.
  28. Lloyd R.J., Pritchard G.G., Characterization of X-prolyl-dipeptidyl aminopeptidase from Lactococcus lactis subsp. lactis, J. Gen. Microbiol. 137 (1991) 49-55.
  29. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J., Protein measurement with the folin phenol reagent, J. Biol. Chem. 193 (1951) 265-276.
  30. Marteau P., Rambaud J.-C., Potential of using lactic acid bacteria for therapy and immunomodulation in man, FEMS Microbiol. Rev. 12 (1993) 207-220.
  31. Matos J., Nardi M., Kumura H., Monnet V., Genetic characterization of pepP, which encodes an aminopeptidase P whose deficiency does not affect Lactococcus lactis growth in milk, unlike deficiency of the X-prolyl dipeptidyl aminopeptidase, Appl. Environ. Microbiol. 64 (1998) 4591-4595.
  32. Mayo B., Kok J., Venema K., Bockelmann W., Teuber M., Reinke H. Venema G., Molecular cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene from Lactococcus lactis subsp. cremoris, Appl. Environ. Microbiol. 57 (1991) 38-44.
  33. McSweeney P.L.H., Sousa M.J., Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review, Lait 80 (2000) 293-324.
  34. Meyer J., Jordi R., Purification and characterization of X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus lactis and from Streptococcus thermophilus, J. Dairy Sci. 70 (1987) 738-745.
  35. Meyer-Barton E.C., Klein J.R., Imam M., Plapp R., Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrueckii ssp. lactis DSM7290, Appl. Microbiol. Biotechnol. 40 (1993) 82-89.
  36. Mierau I., Kunji E.R.S., Leenhouts K.J., Hellendoorn M.A., Haandrikman A.J., Poolman B., Konings W.N., Venema G., Kok J., Multiple peptidase mutants of Lactococcus lactis are severely impaired in their ability to grow in milk, J. Bacteriol. 178 (1996) 2794-2803.
  37. Mierau I., Kunji E.R., Venema G., Kok J., Casein and peptide degradation in lactic acid bacteria, Biotechnol. Genet. Eng. Rev. 14 (1997) 279-301.
  38. Miller G.C., Mackinnon K., Peptidase mutants of Salmonella typhimurium, J. Bacteriol. 120 (1974) 355-363.
  39. Miyakawa H., Kobayashi S., Shimamura S., Tomita M., Purification and characterization of an X-prolyl-dipeptidyl aminopeptidase from Lactobacillus delbrueckii ssp. bulgaricus LBU-147, J. Dairy Sci. 74 (1991) 2375-2381.
  40. Miyakawa H., Hashimoto I., Nakamura T., Ishibashi N., Shimamura S., Igoshi K., Purification and characterization of an X-prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus LHE-511, Milchwissenschaft 49 (1994) 670-673.
  41. Monnet V., Oligopeptidases from Lactococcus lactis, Methods Enzymol. 248 (1995) 579-592.
  42. Nardi, M., Chopin M.C., Cals M.M., Gripon J.C., Cloning and DNA-sequence analysis of an X-prolyl-dipeptidyl-aminopeptidase gene from Lactococcus lactis ssp. lactis NCDO 763, Appl. Environ. Microbiol. 57 (1991) 45-50.
  43. Pritchard G.C., Coolbear T., The physiology and biochemistry of the proteolytic system in lactic acid bacteria, FEMS Microbiol. Rev. 12 (1993) 179-206.
  44. Rosenberg M., Court D., Regulatory sequences involved in the promotion and termination of RNA transcription, Annu. Rev. Genet. 13 (1979) 319-353.
  45. Rul F., Monnet V., Presence of additional peptidases in Streptococcus thermophilus CNRZ 302 compared to Lactococcus lactis, J. Appl. Microbiol. 82 (1997) 695-704.
  46. Sambrook J., Fritch E.F., Maniatis T., Molecular cloning. A laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, New York, USA, 1989.
  47. Steele J.L., Ünlü G., Impact of lactic acid bacteria on cheese flavor development, Food Technol. 46 (1992) 128-130.
  48. Stiles M.E., Biopreservation by lactic acid bacteria, Antonie Leeuwenhoek 70 (1996) 331-345.
  49. Tannock G.W., Probiotic properties of lactic-acid bacteria: plenty of scope for fundamental R & D, Trends Biotechnol. 15 (1997) 270-274.
  50. Thomas T.D., Pritchard G.G., Proteolytic enzymes of dairy starter cultures, FEMS Microbiol. Rev. 46 (1987) 245-268.
  51. Tsakalidou E., Anastasiou R., Papadimitriou K., Manolopoulou E., Kalantzopoulos G., Purification and characterisation of an intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4, J. Biotechnol. 59 (1997) 203-211.
  52. Tsakalidou E., Zoidou E., Pot B., Wassil L., Ludwig W., Devriese L.A., Kalantzopoulos G., Schleifer K.H., Kersters K., Identification of streptococci from Greek Kasseri cheese and description of Streptococcus macedonicus sp. nov, Int. J. Syst. Bacteriol. 48 (1998) 519-527.
  53. Varmanen P., Savijoki K., Åval S., Palva A., Tynkkynen S., X-Prolyl dipeptidyl amino- peptidase gene (pepX) is part of the glnRA operon in Lactobacillus rhamnosus, J. Bacteriol. 182 (2000) 146-154.
  54. Vesanto E., Savijoki K., Rantanen T., Steele J.L., Palva A., An X-prolyl-dipeptidyl aminopeptidase (pepX) gene from Lactobacillus helveticus, Microbiology 141 (1995) 3067-3075.
  55. Yan T.R., Ho S.C., Hou C.L., Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR, Biosci. Biotechnol. Biochem. 56 (1992) 704-707.
  56. Yüksel G.Ü., Steele J.L., DNA sequence analysis, expression, distribution, and physiological role of the Xaa-prolyldipeptidyl aminopeptidase gene from Lactobacillus helveticus CNRZ32, Appl. Microbiol. Biotechnol. 44 (1996) 766-773.
  57. Zevaco C., Monnet V., Gripon J.-C., Intracellular X-prolyl-dipeptidyl peptidase from Lactococcus lactis ssp. lactis: purification and properties, J. Appl. Bacteriol. 68 (1990) 357-366.

Abstract

Copyright INRA, EDP Sciences

Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.

Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.

Initial download of the metrics may take a while.