Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Merieau, Annabelle; Gügi, Bruno; Guespin‐Michel, Janine; Orange, Nicole

doi:10.1007/bf00166857

Cited by 30 publications

(27 citation statements)

References 17 publications

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“…At 17°C, changes in various properties were observed in P. Xuorescens: the production of secreted enzymes was maximal [14,21], causing diYculties in extracting outer membranes of the bacteria. Moreover, the permeability of the outer membrane to the -lactamine mezlocillin is modiWed around 17°C, via the channel size of major porin OprF [22].…”

Section: Resultsmentioning

confidence: 98%

Growth temperature and OprF porin affect cell surface physicochemical properties and adhesive capacities of Pseudomonas fluorescens MF37

Hémery¹,

Chevalier²,

Bellon‐Fontaine³

et al. 2006

J Ind Microbiol Biotechnol

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Pseudomonads adapt to various ecological niches by forming biofilms, which first requires bacterial adhesion on surfaces. We studied the influence of growth temperature on surface physicochemical properties of Pseudomonas fluorescens MF37 and on its adhesive capacities onto inert surfaces. It presented a global hydrophilic character, measured by microbial adhesion to solvent (MATS), and showed a cell surface more hydrophilic at 8 and 28 degrees C than at 17 degrees C. Moreover, P. fluorescens MF37 was more adhesive at 17 degrees C. This critical temperature thus should be carefully taken into account in food safety. Adhesion onto inert surfaces is thus influenced by the growth temperature, which modifies the bacteria cell wall properties through changes in the outer membrane components. Therefore, we studied the effect of the loss of OprF, the major outer membrane protein, known to act as an adhesin (root, and endothelial cells). The OprF-deficient mutant was able to adhere to surfaces, but showed the same physicochemical and adhesion properties on abiotic surfaces whatever the growth temperature. OprF is thus not essential in this adhesion process. However, we suggest that OprF is involved in the bacterial environmental temperature sensing by P. fluorescens.

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Section: Resultsmentioning

confidence: 98%

Growth temperature and OprF porin affect cell surface physicochemical properties and adhesive capacities of Pseudomonas fluorescens MF37

Hémery¹,

Chevalier²,

Bellon‐Fontaine³

et al. 2006

J Ind Microbiol Biotechnol

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“…Moreover, our most striking result is the finding that the temperature at which maximum production of PLI and PLIII occurs on two different media coincides with the critical temperature for growth on these media. A coincidence between the temperature at which maximum production of extracellular enzymes occurs (which is lower than the temperature required for optimal growth) and the critical temperature for growth has been demonstrated only for strains of P. fluorescens (12,13,15,22), for which only one critical temperature was observed. In addition, when each enzyme is considered, both PLI and PLIII have two different temperatures at which maximum production occurs, depending on the culture medium, which are the same temperatures as the two critical temperatures for growth.…”

Section: Discussionmentioning

confidence: 99%

“…More recently, production of several enzymes by different strains of Pseudomonas fluorescens was described as being optimal at one temperature, 17°C (12,15,22). The physiological importance of this temperature was later emphasized when Guillou and Guespin-Michel showed that it separates two temperature domains in which the maximum specific growth rate depends on temperature (13).…”

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confidence: 99%

Production of Pectate Lyases and Cellulases by Chryseomonas luteola Strain MFCL0 Depends on the Growth Temperature and the Nature of the Culture Medium: Evidence for Two Critical Temperatures

Praly

Buchon

Guespin‐Michel

et al. 2000

Appl Environ Microbiol

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Several extracellular enzymes that are responsible for plant tissue maceration were detected in culture supernatant of the psychrotrophic bacterium Chryseomonas luteola MFCL0. Isoelectrofocusing experiments showed that pectate lyase (PL) activity resulted from the cumulative action of three major isoenzymes, designated PLI, PLII, and PLIII. Cellulolytic activity was also detected in culture supernatants. These enzymes exhibited different behaviors with respect to growth temperature. PLII was not regulated by temperature, whereas PLI and PLIII were regulated similarly by growth temperature. Maximal levels of PLI and PLIII were produced at 14°C when cells were grown in polygalacturonate-containing synthetic medium and at around 20 to 24°C in nutrient broth. In contrast, thermoregulation of cellulolytic activity production differed from thermoregulation of PL. The level of cellulolytic activity was low in all media at temperatures up to 20°C, and then it increased dramatically until the temperature was 28°C, which is the optimal temperature for growth of C. luteola. Previously, we defined the critical temperature by using the modified Arrhenius equation to characterize bacterial behavior. This approach consists of monitoring changes in the maximal specific growth rate as a function of temperature. Our most striking result was the finding that the temperature at which maximum levels of PLI and PLIII were produced in two different media was the same as the critical temperature for growth observed in these two media.The most general method for fresh food preservation is cold storage. The main drawback of this method is psychrotrophic bacteria that produce extracellular spoilage enzymes even at low temperatures (5). Psychrotrophic bacteria grow at a wide range of temperatures (from 0 to 35°C, with an optimum temperature of approximately 30°C according to Morita [23]). Chryseomonas luteola MFCL0 has been isolated from spoiled celeriac stored at low temperatures. This bacterium, which has not been described as a phytopathogen yet, is able to macerate plant tissue even at low temperatures, which suggests that extracellular spoilage enzymes are produced under these conditions.Many fungi and bacteria cause soft rot of plant products during storage. These microorganisms produce pectinolytic and cellulolytic enzymes that macerate plant tissue (20, 24). Several pectinases have been characterized; these enzymes include pectate lyases (PL), pectin lyases, and polygalacturonases. PL and pectin lyases catalyze cleavage of the ␣-1,4 bond between galacturonic acid residues by ␤-elimination, generating unsaturated products (C 4 to C 5 ), while polygalacturonases hydrolyze their substrates. PL are distinguished from pectin lyases by their specificity for pectin that has been demethylated by pectin methyl esterases (8,26,28). Studies of cellulases (Cel) have revealed a number of cellulolytic enzymes that act together to degrade cellulose in plant cell walls (3, 29). These enzymes have been found previously in mesophilic bacteria, such ...

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“…It has been demonstrated that at least two strains of P. fluorescens (B52 and LS107d2) secrete only a single detectable lipase of approximately 52 kDa, since site-specific mutants are phenotypically lipase negative and this study). The regulation of lipase production is of particular interest in that there is an inverse relationship between enzyme production and growth temperature in cultures growing in steady state (Andersson, 1980 ;Merieau et al, 1993) …”

Section: Introductionmentioning

confidence: 99%

The aprX–lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production The GenBank accession numbers for the sequences reported in this paper are AF216700, AF216701 and AF216702.

et al. 2001

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Extracellular protease and lipase production by psychrotrophic strains of Pseudomonas fluorescens is repressed by iron and regulated by temperature. The regulation of protease and lipase has been investigated in P. fluorescens B52. Whereas lipase production is increased below the optimum growth temperature (' low-temperature regulation '), protease production was relatively constant and only decreased above the optimum growth temperature. The genes encoding protease (aprX) and lipase (lipA) are encoded at opposite ends of a contiguous set of genes which also includes protease inhibitor, Type I secretion functions and two autotransporter proteins. Evidence is presented indicating that these genes constitute an operon, with a promoter adjacent to aprX which has been identified by S1 nuclease analysis. The regulation of aprX and lipA has been investigated at the RNA level and using lacZ fusion strains. Whereas the data are consistent with iron regulation at the transcriptional level, a lipA'-'lacZ fusion is not regulated by temperature, suggesting that temperature regulation is post-transcriptional or post-translational. The possibility of regulation at the level of mRNA decay is discussed.

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Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Cited by 30 publications

References 17 publications

Growth temperature and OprF porin affect cell surface physicochemical properties and adhesive capacities of Pseudomonas fluorescens MF37

Growth temperature and OprF porin affect cell surface physicochemical properties and adhesive capacities of Pseudomonas fluorescens MF37

Production of Pectate Lyases and Cellulases by Chryseomonas luteola Strain MFCL0 Depends on the Growth Temperature and the Nature of the Culture Medium: Evidence for Two Critical Temperatures

The aprX–lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production The GenBank accession numbers for the sequences reported in this paper are AF216700, AF216701 and AF216702.

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