Cold‐Adapted Microorganisms: Adaptation Strategies and Biotechnological Potential

Margesin, Rosa; Feller, Georges; Gerday, Charles; Russell, Nick J.

doi:10.1002/0471263397.env150

Cited by 49 publications

(62 citation statements)

References 103 publications

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“…During the past decade it has been recognized that cold-adapted microorganisms provide a wide biotechnological potential, offering numerous economic and ecological advantages over the use of organisms and their enzymes which operate at higher temperatures (Brenchley, 1996;Gerday et al, 2000;Margesin et al, 2002;Soriano et al, 2000). Cold-active enzymes are characterized by high catalytic effi ciency at low and moderate temperatures at which homologous mesophilic enzymes are not active, and are thermolabile (Margesin et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

Kuddus

Ramteke

2008

J. Gen. Appl. Microbiol.

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A novel psychro-tolerant bacterium, Curtobacterium luteum, secreting an extracellular protease was isolated from the soil of Gangotri glacier, Western Himalaya. Maximum enzyme production was achieved when the strain was grown in a pH-neutral medium containing skim milk at 15 C over 120 h. The metal ions such as Zn 2+ and Cr 2+ enhanced enzyme production. The specifi c activity of purifi ed enzyme was 8,090 units/mg after 34.1-fold purifi cation. The 115 kDa enzyme was a metalloprotease (activity inhibited by EDTA and EGTA) and showed maximum activity at 20 C and pH 7. The enzyme was active over a broad pH range and retained 84% of its original activity between pH 6 and 8. There was no loss in enzyme activity when exposed for 3 h at 4

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Section: Introductionmentioning

confidence: 99%

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

Kuddus

Ramteke

2008

J. Gen. Appl. Microbiol.

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“…At the other end of the temperature scale, metabolically active psychrophilic bacteria have been detected in liquid brine veins of sea ice at Ϫ20°C (4). These cold-loving microorganisms face the thermodynamic challenge to maintain enzyme-catalyzed reactions and metabolic rates compatible with sustained growth near or below the freezing point of pure water (5,6). Directed evolution experiments have highlighted that, in theory, cold activity of enzymes can be gained by several subtle adjustments of the protein structure (7).…”

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confidence: 99%

Activity-Stability Relationships in Extremophilic Enzymes

D’Amico

Marx

Gerday

et al. 2003

Journal of Biological Chemistry

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Psychrophilic, mesophilic, and thermophilic ␣-amylases have been studied as regards their conformational stability, heat inactivation, irreversible unfolding, activation parameters of the reaction, properties of the enzyme in complex with a transition state analog, and structural permeability. These data allowed us to propose an energy landscape for a family of extremophilic enzymes based on the folding funnel model, integrating the main differences in conformational energy, cooperativity of protein unfolding, and temperature dependence of the activity. In particular, the shape of the funnel bottom, which depicts the stability of the native state ensemble, also accounts for the thermodynamic parameters of activation that characterize these extremophilic enzymes, therefore providing a rational basis for stability-activity relationships in protein adaptation to extreme temperatures.Our planet harbors a huge number of harsh environments that are considered as "extreme" from an anthropocentric point of view, as far as temperature, pH, osmolarity, free water, or pressure are concerned. Nevertheless, these peculiar biotopes have been successfully colonized by numerous organisms, mainly extremophilic bacteria and archaea. As the curiosity of scientists stimulates the exploration of new environments, it seems that there is no "empty space" for life on Earth and, for instance, even the supercooled cloud droplets contain actively growing bacteria (1). Among the extremophilic microorganisms, those living at extreme temperatures have attracted much attention. Thermophiles have revealed the unsuspected upper temperature for life at about 113°C (2, 3). Their enzymes have also demonstrated a considerable biotechnological potential such as the various thermostable DNA polymerases used in PCR that have boosted many laboratory techniques. At the other end of the temperature scale, metabolically active psychrophilic bacteria have been detected in liquid brine veins of sea ice at Ϫ20°C (4). These cold-loving microorganisms face the thermodynamic challenge to maintain enzyme-catalyzed reactions and metabolic rates compatible with sustained growth near or below the freezing point of pure water (5, 6). Directed evolution experiments have highlighted that, in theory, cold activity of enzymes can be gained by several subtle adjustments of the protein structure (7). However, in natural cold environments, the consensus for the adaptive strategy is to take advantage of the lack of selective pressure for stable proteins for losing stability, therefore making the enzyme more mobile or flexible at temperatures that "freeze" molecular motions and reaction rates (8).The crystal structures of extremophilic enzymes unambiguously indicate a continuum in the molecular adaptations to temperature. There is indeed a clear increase in the number and strength of all known weak interactions and structural factors involved in protein stability from psychrophiles to mesophiles (living at intermediate temperatures close to 37°C) and to thermophiles (2, 9 -1...

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“…Suutari and Laakso reported that at low temperature the ratio of unsaturated fatty acids to saturated fatty acids is increased in the membrane. It can modulate the activities of the enzymes involved in fatty acid and lipid biosynthesis [21] and help to synthesis the short-chain fatty acids, branched chain fatty acids and anteiso-fatty acids to long chain fatty acids, straight-chain fatty acids and iso fatty acids respectively [22]. Some investigators believed that cryoprotectants prevent the cold induced aggregation of proteins and maintain the optimum membrane fluidity even at low temperature.…”

Section: Cryo -Defense Strategy Of Marine Cold Loving Microorganismsmentioning

confidence: 99%

“…Thus the major drawback in the use of cold proteases for such purposes is their weak stability at temperatures higher than 25°C. However, in recent years with the growing interest on cold enzymes, researchers are focusing more on the thermal stability and molecular adaptation of these protein molecules [44,45]. Taguchi demonstrated that sequential random mutagenesis exhibited 70% higher catalytic efficiency in comparision with wild type at 10°C when Pro-L-Phe-p-nitroanilide was used as a synthetic substrate.…”

Section: Enzymes From Marine Cold Loving Microorganismsmentioning

confidence: 99%

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Psychrozymes- The Next Generation Industrial Enzymes

Pulicherla¹,

Ghosh²,

Kumar³

et al. 2011

J Marine Sci Res Development

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The earth is dominated by low-temperature environments. Over 80% of the earth's biosphere is cold, and about 90% of the oceans are colder than 5°C. This cold marine environment is characterized by challenging conditions for the survival of native microorganisms and are classified as psychrophilic or psychrotolerant organisms. The biocatalysts, produced by these microorganisms are called as cold adapted enzymes, function under extreme cold condition and display a high specificity. It is associated with a relatively extreme stability provides new opportunities for the potential application of these cold adapted enzymes in various industrials processes. The main objective of current review is to discuss the sources, possible industrial applications and current scenario of the cold adapted enzymes.

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Cold‐Adapted Microorganisms: Adaptation Strategies and Biotechnological Potential

Abstract: Cold‐Adapted Microorganisms—Definition Ecology Mechanisms of Adaptation to Cold Biotechnological Potential

Cited by 49 publications

References 103 publications

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

Activity-Stability Relationships in Extremophilic Enzymes

Psychrozymes- The Next Generation Industrial Enzymes

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