This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hebert, E. M.
Right arrow Articles by De Giori, G. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hebert, E. M.
Right arrow Articles by De Giori, G. S.
Agricola
Right arrow Articles by Hebert, E. M.
Right arrow Articles by De Giori, G. S.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, December 2000, p. 5316-5321, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Nutritional Requirements and Nitrogen-Dependent Regulation of Proteinase Activity of Lactobacillus helveticus CRL 1062

Elvira M. Hebert,1 Raul R. Raya,1 and Graciela S. De Giori1,2,*

Centro de Referencia para Lactobacilos (CERELA), CONICET,1 and Cátedra de Microbiología Superior, Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán,2 4000 San Miguel de Tucuman, Argentina

Received 30 May 2000/Accepted 19 September 2000

The nutritional requirements of Lactobacillus helveticus CRL 1062 were determined with a simplified chemically defined medium (SCDM) and compared with those of L. helveticus CRL 974 (ATCC 15009). Both strains were found to be prototrophic for alanine, glycine, asparagine, glutamine, and cysteine. In addition, CRL 1062 also showed prototrophy for lysine and serine. The microorganisms also required riboflavin, calcium pantothenate, pyridoxal, nicotinic acid, and uracil for growth in liquid SCDM. The growth rate and the synthesis of their cell membrane-bound serine proteinases, but not of their intracellular leucyl-aminopeptidases, were influenced by the peptide content of the medium. The highest proteinase levels were found during cell growth in basal SCDM, while the synthesis of this enzyme was inhibited in SCDM supplemented with Casitone, Casamino Acids, or beta -casein. Low-molecular-mass peptides (<3,000 Da), extracted from Casitone, and the dipeptide leucylproline (final concentration, 5 mM) play important roles in the medium-dependent regulation of proteinase activity. The addition of the dipeptide leucylproline (5 mM) to SCDM reduced proteinase activity by 25%.

* Corresponding author. Mailing address: CERELA, Chacabuco 145, 4000 San Miguel de Tucumán, Argentina. Phone: 54-381-4310465. Fax: 54-381-4310465. E-mail: gsayoy{at}cerela.org.ar.

Applied and Environmental Microbiology, December 2000, p. 5316-5321, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hebert, E. M., Mamone, G., Picariello, G., Raya, R. R., Savoy, G., Ferranti, P., Addeo, F. (2008). Characterization of the Pattern of {alpha}s1- and {beta}-Casein Breakdown and Release of a Bioactive Peptide by a Cell Envelope Proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Appl. Environ. Microbiol. 74: 3682-3689 [Abstract] [Full Text]  
  • Medina, M., Villena, J., Vintini, E., Hebert, E. M., Raya, R., Alvarez, S. (2008). Nasal Immunization with Lactococcus lactis Expressing the Pneumococcal Protective Protein A Induces Protective Immunity in Mice. Infect. Immun. 76: 2696-2705 [Abstract] [Full Text]  
  • Christiansen, J. K., Hughes, J. E., Welker, D. L., Rodriguez, B. T., Steele, J. L., Broadbent, J. R. (2008). Phenotypic and Genotypic Analysis of Amino Acid Auxotrophy in Lactobacillus helveticus CNRZ 32. Appl. Environ. Microbiol. 74: 416-423 [Abstract] [Full Text]  
  • Juille, O., Bars, D. L., Juillard, V. (2005). The specificity of oligopeptide transport by Streptococcus thermophilus resembles that of Lactococcus lactis and not that of pathogenic streptococci. Microbiology 151: 1987-1994 [Abstract] [Full Text]  
  • Pastar, I., Tonic, I., Golic, N., Kojic, M., van Kranenburg, R., Kleerebezem, M., Topisirovic, L., Jovanovic, G. (2003). Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10. Appl. Environ. Microbiol. 69: 5802-5811 [Abstract] [Full Text]  
  • Vermeirssen, V., Van Camp, J., Decroos, K., Van Wijmelbeke, L., Verstraete, W. (2003). The Impact of Fermentation and In Vitro Digestion on the Formation of Angiotensin-I-Converting Enzyme Inhibitory Activity from Pea and Whey Protein. J DAIRY SCI 86: 429-438 [Abstract] [Full Text]  
  • Courtin, P., Monnet, V., Rul, F. (2002). Cell-wall proteinases PrtS and PrtB have a different role in Streptococcus thermophilus/Lactobacillus bulgaricus mixed cultures in milk. Microbiology 148: 3413-3421 [Abstract] [Full Text]  
  • Hebert, E. M., De Giori, G. S., Raya, R. R. (2001). Isolation and Characterization of a Slowly Milk-Coagulating Variant of Lactobacillus helveticus Deficient in Purine Biosynthesis. Appl. Environ. Microbiol. 67: 1846-1850 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»