Temperature dependence of growth, enzyme secretion and activity of psychrophilic Antarctic bacteria

Feller, Georges; Narinx, Emmanuel; Arpigny, Jean Louis; Zekhnini, Z.; Swings, Jean; Gerday, Charles

doi:10.1007/bf00212261

Cited by 6 publications

(6 citation statements)

References 6 publications

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“…Evolution has allowed these cold‐adapted organisms, called psychrophiles, not to merely survive, but to breed and grow successfully in the restrictive conditions of cold habitats. Psychrophiles display metabolic fluxes at low temperatures that are more or less comparable to those exhibited by closely related mesophiles living at moderate temperatures [3–8], clearly showing that mechanisms of temperature adaptations are involved. Such mechanisms include a vast array of structural and physiological adjustments in order to cope with the reduction of chemical reaction rates induced by low temperatures.…”

Section: Introductionmentioning

confidence: 91%

Some like it cold: biocatalysis at low temperatures

et al. 2004

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In the last few years, increased attention has been focused on a class of organisms called psychrophiles. These organisms, hosts of permanently cold habitats, often display metabolic fluxes more or less comparable to those exhibited by mesophilic organisms at moderate temperatures. Psychrophiles have evolved by producing, among other peculiarities, "cold-adapted" enzymes which have the properties to cope with the reduction of chemical reaction rates induced by low temperatures. Thermal compensation in these enzymes is reached, in most cases, through a high catalytic efficiency associated, however, with a low thermal stability. Thanks to recent advances provided by X-ray crystallography, structure modelling, protein engineering and biophysical studies, the adaptation strategies are beginning to be understood. The emerging picture suggests that psychrophilic enzymes are characterized by an improved flexibility of the structural components involved in the catalytic cycle, whereas other protein regions, if not implicated in catalysis, may be even more rigid than their mesophilic counterparts. Due to their attractive properties, i.e., a high specific activity and a low thermal stability, these enzymes constitute a tremendous potential for fundamental research and biotechnological applications.

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Section: Introductionmentioning

confidence: 91%

Some like it cold: biocatalysis at low temperatures

et al. 2004

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“…Conditions that maximize the specific cell growth rate are often in compromise with those that maximize the specific rate of enzyme production (Gordillo et al 1998). In fact, it is usual that pH (Illanes et al 1988a;McDermid et al 1988), temperature (Akinrefon 1969;Feller et al 1994) and the level of dissolved oxygen (García-Garibay et al 1987; Barberis and Gentina 1998) optimal for growth differ from the corresponding optima for enzyme production. Compromise values are often used, but impressive increases in enzyme productivity have been reported by profiling these variables during cell culture (Mukhopadhyay and Malik 1980;Mukhopadhyay 1981;Ioniţȃ et al 2001).…”

Section: Enzyme Synthesismentioning

confidence: 99%

Enzyme Production

Illanes

2008

Enzyme Biocatalysis

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“…2003; Zeng et al. 2004); some of these enzymes have been isolated from Antarctic micro‐organisms (Feller et al. 1994; Kulakova et al.…”

Section: Introductionmentioning

confidence: 99%

Lipolytic activity of Antarctic cold-adapted marine bacteria (Terra Nova Bay, Ross Sea)

et al. 2006

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Aims: The aim of this study was to investigate the lipolytic activity of cold‐adapted Antarctic marine bacteria and, furthermore, the combined effect of some environmental factors on this enzymatic process. Methods and Results: Strains were assayed for lipolytic activity on a basal medium amended with seven individual fatty acid esters. A significant activity was observed for 148 isolates (95·5% of the total screened). The interactive effect of pH, temperature and NaCl concentration on the substrates was tested for six representative isolates, identified as Pseudoalteromonas, Psychrobacter and Vibrio. Differences between strains according to NaCl and pH tolerances were observed. Only one strain degraded the substrate more efficiently at 4°C than at 15°C. Conclusions: Our findings demonstrate that the lipolytic activity of Antarctic marine bacteria is rather variable, depending on culture conditions, and occurs in a wide range of salt concentration and pH. Significance and Impact of the Study: Isolation and characterization of bacteria that are able to efficiently remove lipids at low temperatures will provide insight into the possibility to use cold‐adapted bacteria as a source of exploitable enzymes. Moreover, research on the interactive effects of salt concentration, pH and temperature will be useful to understand the true enzyme potentialities for industrial applications.

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Temperature dependence of growth, enzyme secretion and activity of psychrophilic Antarctic bacteria

Cited by 6 publications

References 6 publications

Some like it cold: biocatalysis at low temperatures

Some like it cold: biocatalysis at low temperatures

Enzyme Production

Lipolytic activity of Antarctic cold-adapted marine bacteria (Terra Nova Bay, Ross Sea)

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