Hostname: page-component-76fb5796d-25wd4 Total loading time: 0 Render date: 2024-04-25T12:37:20.822Z Has data issue: false hasContentIssue false
  • English
  • Français

Repression of Pseudomonas fluorescens extracellular lipase secretion by arginine

Published online by Cambridge University Press:  01 June 2009

Leonides Fernandez ,
Carmen San Jose  and
Robin C. McKellar
Leonides Fernandez
Affiliation:
Departamento de Tecnologia y Bioquimica de los Alimentos, Facultad de Veterinaria, Ciudad Universitaria, 28040-Madrid, Spain
Carmen San Jose
Affiliation:
Departamento de Tecnologia y Bioquimica de los Alimentos, Facultad de Veterinaria, Ciudad Universitaria, 28040-Madrid, Spain
Robin C. McKellar
Affiliation:
Food Research Centre, Research Branch, Agriculture Canada, Ottawa KlA 0C6, Canada
Get access Rights & Permissions [Opens in a new window]

Summary

The effect of arginine on the production of extracellular lipase by Pseudomonas fluorescens 32A was studied. Arginine repressed lipase production when N was supplied partially or totally as arginine. Proteinase production was unaffected under the same conditions. Arginine did not repress lipase secretion when cells were pregrown in an arginine-containing medium; however, repression was found with uninduced cells. Several arginine-analogues were tested for the ability to repress lipase secretion and. of these, L-homoarginine and L-canavanine were the most effective. D-Arginine, L-arginine methyl ester, and L-ornithine did not cause repression. With the exception of glutamic acid and methionine, those amino acids that supplied N but not C for growth were found to repress lipase secretion. It is suggested that the accumulation of metabolic intermediate(s) may cause repression of lipase production.

Type
Original Articles
Information
Journal of Dairy Research , Volume 57 , Issue 1 , February 1990 , pp. 69 - 78
Copyright
Copyright © Proprietors of Journal of Dairy Research 1990

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Alford, J. A. & Pierce, D. A. 1963 Production of lipase by Pseudomonas fragi in a synthetic medium. Journal of Bacteriology 86 24–29CrossRefGoogle Scholar
Clarke, P. & Ornston, N. 1975 Metabolic pathways and regulation: II. In Genetics and Biochemistry of Pseudomonas pp. 203–340 (Eds Clarke, P. H. and Richmond, M. H.). New York: WileyGoogle Scholar
Fairbairn, D. J. & Law, B. A. 1986 Proteinases of psychrotrophic bacteria: their production, properties, effects and control. Journal of Dairy Research 53 139–177CrossRefGoogle ScholarPubMed
Fairbairn, D. J. & Law, B. A. 1987 The effect of nitrogen and carbon sources on proteinase production by Pseudomonas fluorescens. Journal of Applied Bacteriology 62 105–113Google Scholar
Griffiths, M. W. & Phillips, J. D. 1984 Effect of aeration on extracellular enzyme synthesis by psychrotrophs growing in milk during refrigerated storage. Journal of Food Protection 47 697–702CrossRefGoogle ScholarPubMed
Harder, W. 1979 Regulation of the synthesis of extracellular enzymes in microorganisms. Society of General Microbiology Quarterly 6 139–140Google Scholar
Himelbloom, B. H. & Hassan, H. M. 1986 Effects of cysteine on growth, protease production, and catalase activity of Pseudomonas fluorescens. Applied and Environmental Microbiology 51 418–421Google Scholar
Kalyankar, G. D., Ikawa, M. & Snell, E. E. 1958 The enzymatic cleavage of canavanine to homoserine and hydroxyguaninine. Journal of Biological Chemistry 233 1175–1178Google Scholar
Law, B. A. & Fairbairn, D. J. 1985 Factors controlling proteinase production by psychrotrophic baeteria. National Institute for Research in Dairying Final Report 1984–5 p. 181Google Scholar
Litchfield, C. D. & Prescott, J. M. 1970 Regulation of proteolytic enzyme production by Aeromonas proteolytica I. Extracellular endopeptidase. Canadian Journal of Microbiology 16 17–22CrossRefGoogle ScholarPubMed
McKellar, R. C. 1982 Factors influencing the production of extracellular proteinase by Pseudomonas fluorescens. Journal of Applied Bacteriology 53 305–316CrossRefGoogle ScholarPubMed
McKellar, R. C. 1986 A rapid colorimetric assay for the extracellular lipase of Pseudomonas fluorescens B52 using β-naphthyl caprylate. Journal of Dairy Research 53 117–127Google Scholar
McKellar, B. C. & Cholette, H. 1985 Inhibition by chelating agents of the formation of active extracellular proteinase by Pseudomonas fluorescens 32A. Journal of Dairy Research 52 91–100CrossRefGoogle ScholarPubMed
McKellar, R. C., Shamsuzzaman, K., San Jose, C. & Cholette, H. 1987 Influence of iron(III) and pyoverdine, a siderophore produced by Pseudomonas fluorescens B52, on its extracellular proteinase and lipase production. Archives of Microbiology 147 225–230Google Scholar
Nakai, S., Koide, K. & Eugster, K. 1984 A new mapping super-simplex optimisation for food product and process development. Journal of Food Science 49 1143–1148Google Scholar
Paquette, G. J. & McKellar, R. C. 1986 Optimization of extracellular lipase activity from Pseudomonas fluorescens using a Super-Simplex Optimization program. Journal of Food Science 51 655–658Google Scholar
Patel, T. R., Bartlett, F. M. & Hamid, J. 1983 Extracellular heat-resistant proteases of psychrotrophic pseudomonads. Journal of Food Protection 46 90–94Google Scholar
Richmond, M. H. 1959 The differential effect of arginine and canavanine on growth and enzyme formation in Staphylococcus aureus 524 SC. Biochemical Journal 73 155–167CrossRefGoogle ScholarPubMed
Rowe, M. T. 1988 Effect of carbon dioxide on growth and extracellular enzyme production by Pseudomonas fluorescens B52. international Journal of Food Microbiology 6 51–56Google Scholar
Rowe, M. T. & Gilmour, A. 1983 Nutritional factors affecting extracellular enzyme production by Pseudomonas fluorescens B52. Milchwissenschaft 38 705–707Google Scholar
Schachtele, C. F. & Rogers, P. 1965 Canavanine death in Escherichia coli. Journal of Molecular Biology 14 474–489CrossRefGoogle ScholarPubMed
Schwartz, J. H. & Maas, W. K. 1960 Analysis of the inhibition of growth produced by canavanine in Escherichia coli. Journal of Bacteriology 79 794–799Google Scholar
Stalon, V. & Mercenier, A. 1984 L-Arginine utilization by Pseudomonas species. Journal of General Microbiology 130 69–76Google ScholarPubMed
Stead, D. 1985 Factors controlling lipase production by psychrotrophic bacteria. National Institute for Research in Dairying Final Report 1984–5 p. 181Google Scholar
Stead, D. 1986 Microbial lipases: their characteristics, role in food spoilage and industrial uses. Journal of Dairy Research 53 481–505Google Scholar
Stead, D. 1987 Production of extracellular lipases and proteinases during prolonged growth of strains of psychrotrophic bacteria in whole milk. Journal of Dairy Research 54 535–543Google Scholar
Walker, J. B. 1955 Homoarginine inhibition of Escherichia coli B. Journal of Biological Chemistry 212 617–622CrossRefGoogle ScholarPubMed