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Production of extracellular lipases and proteinases during prolonged growth of strains of psychrotrophic bacteria in whole milk

Published online by Cambridge University Press:  01 June 2009

Donald Stead
Donald Stead
Affiliation:
AFRC Institute of Food Research, Reading Laboratory, Shinfield, Reading RG2 9AT, UK
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Summary

Three strains of psychrotrophic Pseudomonas spp., each with different lipolytic and proteolytic phenotypes (including a proteinase-deficient mutant), were cultured separately in whole milk at 7°C. Growth rates were the same during logarithmic growth phase, but during early stationary phase the cell densities were related to the activities of lipase and proteinase in the cultures. Only one strain underwent pronounced death phase. Proteinase activity was not detected in the culture of the proteinase-deficient mutant, but in those of the other strains it increased to a plateau, or continued to increase linearly. Lipase activity of the culture of each strain reached a peak in early stationary phase; in late stationary phase activity was highest for the proteinase-deficient mutant strain where degradation of lipase by bacterial proteinase would have been least. The ability of psychrotrophic bacteria both to survive for long periods and to produce high levels of proteinases and lipases on prolonged incubation in milk emphasizes the spoilage potential arising from psychrotrophic bacteria in inadequately cleaned dairy equipment.

Type
Original Articles
Information
Journal of Dairy Research , Volume 54 , Issue 4 , November 1987 , pp. 535 - 543
Copyright
Copyright © Proprietors of Journal of Dairy Research 1987

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References

REFERENCES

Alichanidis, E., Wratiiall, J. H. M. & Andrews, A. T. 1980 Heat stability of plasmin (milk proteinase) and plasminogen. Journal of Dairy Research 53 259–269CrossRefGoogle Scholar
Andersson, R. E. 1980 Microbial lipolysis at low temperatures. Applied and Environmental Microbioloqy 39 36–40CrossRefGoogle ScholarPubMed
Andersson, R. E., Danielsson, G., Hedlund, C. B. & Svensson, S. G. 1981 Effect of a beat-resistant microbial lipase on flavor of ultra-high-temperature sterilized milk. Journal of Dairy Science 64 375–379CrossRefGoogle Scholar
Andrews, A. T. 1983 Proteinases in normal bovine milk and their action on caseins. Journal of Dairy Research 50 45–55CrossRefGoogle ScholarPubMed
Bucky, A. R., Hayes, P. R. & Robinson, D. S. 1986 Lipase production by a strain of Pseudomonas fluorescens in whole milk and skimmed milk. Food Microbiology 3 37–44CrossRefGoogle Scholar
Cascieri, T. & Mallette, M. F. 1976 a Peptide utilization by Pseudomonas putida and Pseudomonas maltophila. Journal of General Microbiology 92 283–295CrossRefGoogle Scholar
Cascieri, T. & Mallette, M. F. 1976 b Intracellular peptide hydrolysis by Pseudomonas putida and Pseudomonas maltophila. Journal of General Microbiology 92 296–303CrossRefGoogle Scholar
Clarke, P. H. & Ornston, N. 1975 Metabolic pathways and regulation: II. In Genetics and Biochemistry of Pseudomonas pp. 263&340 (Eds Clarke, P. H. and Richmond, M. H.). New York: WileyGoogle Scholar
Cliffe, A. J. & Law, B. A. 1982 A new method for the detection of microbial proteolytic enzymes in milk. Journal of Dairy Research 49 209–219CrossRefGoogle Scholar
Cousin, M. A. 1982 Presence and activity of psychrotrophic microorganisms in milk and dairy products: a review. Journal of Food Protection 45 172–207CrossRefGoogle ScholarPubMed
Cousins, C. M. & Bramley, A. J. 1981 The microbiology of raw milk. In Dairy Microbiology, Vol. 1. The Microbiology of Milk pp. 119&163 (Ed. Robinson, R. K.). London: Applied Science PublishersGoogle Scholar
De Rham, O. & Andrews, A. T. 1982 The roles of native milk proteinase and its zymogen during proteolysis in normal bovine milk. Journal of Dairy Research 49 577–585CrossRefGoogle ScholarPubMed
Dring, R. & Fox, P. F. 1983 Purification and characterization of a heat-stable lipase from Pseudomonas fluorescens AFT 29. Irish Journal of Food Science and Technology 7 157–171Google Scholar
Fairbairn, D. J. 1984 Production and properties of the extracellular proteinase from Pseudomonas fluorescens. Ph.D. thesis, University of ReadingGoogle 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
Fox, P. F. & Stepaniak, L. 1983 Isolation and some properties of extracellular heat-stable lipases from Pseudomonas fluorescens strain AFT 36. Journal of Dairy Research 50 77–89CrossRefGoogle ScholarPubMed
Fryer, T. F., Lawrence, R. C. & Reiter, B. 1967 Methods for isolation and enumeration of lipolytic organisms. Journal of Dairy Science 50 477–484CrossRefGoogle ScholarPubMed
Harrigan, W. F. & McCance, M. E. 1976 Biochemical tests for bacteria. Laboratory Methods in Food and Dairy Microbiology, 2nd edn pp. 67–68. London: Academic PressGoogle Scholar
Jonsson, U. & Snygg, B. G. 1974 Lipase production and activity as a function of incubation time, pH and temperature of four lipolytic micro-organisms. Journal of Applied Bacteriology 37 571–581CrossRefGoogle ScholarPubMed
Jonsson, U. & Snygg, B. G. 1976 [The stability of lipase in the supernatant of Pseudomonas fluorescens as a function of time of incubation and heat treatment.] Chemie Mikrobiologie Technologie der Lebensmittel 4 173–176Google Scholar
Kaminogawa, S., Mizobuchi, H. & Yamauchi, K. 1972 Comparison of bovine milk protease with plasmin. Agricultural and Biological Chemistry 36 2163–2167CrossRefGoogle Scholar
Law, B. A. 1979 Reviews of the progress of dairy science: Enzymes of psychrotrophic bacteria and their effects on milk and milk products. Journal of Dairy Research 46 573–588CrossRefGoogle Scholar
Law, B. A. & Mabbitt, L. A. 1983 New methods for controlling the spoilage of milk and milk products, In Food Microbiology: Advances and Prospects pp. 131–150 (Eds Roberts, T. A. and Skinner, F. A.). LondonAcademic Press (Society for Applied Bacteriology Symposium Series No. 11).Google Scholar
Law, B. A., Sharpe, M. E. & Chapman, H. R. 1976 The effect of lipolytic Gram-negative psychrotrophs in stored milk on the development of rancidity in Cheddar cheese. Journal of Dairy Research 43 459–468CrossRefGoogle Scholar
Lawrence, R. C. 1967 Microbial lipases and related esterases. Part T. Detection, distribution and production of microbial lipases. Dairy Science Abstracts 29 1–8Google Scholar
Lawrence, R. C, Fryer, T. F. & Reiter, B. 1967 The production and characterization of lipases from a micrococcus and a pseudomonad. Journal of General Microbiology 48 401–418CrossRefGoogle Scholar
Murray, S. K., Kwan, K. K. H., Skura, B. J. & McKellar, R. C. 1983 Effect of nitrogen flushing on the production of proteinase by psychrotrophic bacteria in raw milk. Journal of Food Science 48 1166–1169CrossRefGoogle Scholar
Noomen, A. 1975 Proteolytic activity of milk protease in raw and pasteurized cow's milk. Netherlands Milk and Dairy Journal 29 153–161Google Scholar
Patel, T. R. & Jackman, D. M. 1986 Susceptibility of psychrotrophie pseudomonads of milk origin to psychrotrophie bacteriophages. Applied and Environmental Microbiology 51 446–448CrossRefGoogle Scholar
Piton, C. & Richard, J. 1985 [Psychrotrophie pseudomonads in raw milk.] Sciences des Aliments 5 (Hors série IV) 13–16Google Scholar
Richard, J. 1985 [Causes of microbial contamination of milk on the farm and their detection.] Sciences des Aliments 5 (Hors série IV) 9–12Google Scholar
Richter, R. 1981 Microbiological problems in dairy foods in the 1980s. Journal of Food Protection 46 471–475, 479Google Scholar
Speers, J.G.S. & Gilmour, A. 1985 The influence of milk and milk components on the attachment of bacteria to farm dairy equipment surfaces. Journal of Applied Bacteriology 59 325–332CrossRefGoogle ScholarPubMed
Stead, D. 1983 A fluorimetric method for the determination of Pseudomonas fluorescens AR11 lipase in milk.Journal of Dairy Research 50 491–502CrossRefGoogle Scholar
Stead, D. 1986 Microbial lipases: their characteristics, role in food spoilage and industrial uses. Journal of Dairy Research 53 481–505CrossRefGoogle ScholarPubMed
Stead, D. 1987 Assay of proteinases of psychrotrophie bacteria in milk using Hide Powder Azure and a simple procedure for clarification of milk. Journal of Dairy Research 54 295–302CrossRefGoogle Scholar
Stone, L. S. & Zottola, E. A. 1985 Effect of cleaning and sanitizing on the attachment of Pseudomonas fragi to stainless steel. Journal of Food Science 50 951–956CrossRefGoogle Scholar
Thomas, S. B. & Thomas, B. F. 1977 a The bacterial content of milking machines and pipeline milking plants. Part II of a review. Dairy Industries International 42(5) 16, 18–19, 22–23Google Scholar
Thomas, S. B. & Thomas, B. F. 1977 b The bacterial content of milking machines and pipeline milking plants. Part III of a review: Composition of microflora. Dairy Industries International 42(7) 19, 21, 23–25Google Scholar
Thomas, T. D. & Mills, O. E. 1981 Proteolytic enzymes of starter bacteria. Netherlands Milk and Dairy Journal 35 255–273Google Scholar
Torrie, J. P., Cholette, H., Froehlich, D. A. & McKellar, R. C. 1983 Growth of an extracellular proteinase-deficient strain of Pseudomonas fluorescens on milk and milk proteins. Journal of Dairy Research 50 365–374CrossRefGoogle ScholarPubMed
Wretlind, B., Sjöberg, L. & Wadström, T. 1977 Protease-deficient mutants of Pseudomonas aeruginosa: pleiotropic changes in activity of other extracellular enzymes. Journal of General Microbiology 103 329–336CrossRefGoogle ScholarPubMed
Zoltai, P. T., Zottola, E. A. & McKay, L. L. 1981 Scanning electron microscopy of microbial attachment to milk contact surfaces. Journal of Food Protection 44 204–208CrossRefGoogle ScholarPubMed