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Cold-adapted enzymes: mechanisms, engineering and biotechnological application

Bioprocess and Biosystems Engineering, 2023
Most cold-adapted enzymes display high catalytic activity at low temperatures (20-25 °C) and can still maintain more than 40-50% of their maximum activity at lower temperatures (0-10 °C) but are inactivated after a moderate increase in temperature.
Yan, Liu   +5 more
openaire   +2 more sources

Cold Adaptation of Enzyme Reaction Rates

Biochemistry, 2008
A major issue for organisms living at extreme temperatures is to preserve both stability and activity of their enzymes. Cold-adapted enzymes generally have a reduced thermal stability, to counteract freezing, and show a lower enthalpy and a more negative entropy of activation compared to mesophilic and thermophilic homologues.
Sinisa, Bjelic   +2 more
openaire   +2 more sources

Cold-adapted enzymes: from fundamentals to biotechnology

Trends in Biotechnology, 2000
Psychrophilic enzymes produced by cold-adapted microorganisms display a high catalytic efficiency and are most often, if not always, associated with high thermosensitivity. Using X-ray crystallography, these properties are beginning to become understood, and the rules governing their adaptation to cold appear to be relatively diverse.
Gerday, Charles   +13 more
openaire   +3 more sources

Psychrophilic enzymes: hot topics in cold adaptation

Nature Reviews Microbiology, 2003
More than three-quarters of the Earth's surface is occupied by cold ecosystems, including the ocean depths, and polar and alpine regions. These permanently cold environments have been successfully colonized by a class of extremophilic microorganisms that are known as psychrophiles (which literally means cold-loving).
Feller, Georges, Gerday, Charles
openaire   +3 more sources

Cold adapted enzymes

2000
The number of reports on enzymes from cold adapted organisms has increased significantly over the past years, and reveals that adaptive strategies for functioning at low temperature varies among enzymes. However, the high catalytic efficiency at low temperature seems, for the majority of cold active enzymes, to be accompanied by a reduced thermal ...
A O, Smalås   +3 more
openaire   +2 more sources

Computation of enzyme cold adaptation

Nature Reviews Chemistry, 2017
Enzymes that are optimized for low temperatures have characteristics that are distinct from those that operate under milder conditions. This Review examines cold-adapted enzymes and describes how computational studies have highlighted structural and energetic consequences…
Johan Åqvist   +2 more
openaire   +1 more source

Cold-Adapted Enzymes from Marine Antarctic Microorganisms

Marine Biotechnology, 2006
The Antarctic marine environment is characterized by challenging conditions for the survival of native microorganisms. Indeed, next to the temperature effect represented by the Arrhenius law, the viscosity of the medium, which is also significantly enhanced by low temperatures, contributes to slow down reaction rates. This review analyses the different
Marx, J. C.   +4 more
openaire   +3 more sources

Cold-Adapted Enzymes

2001
In the last few years, increased attention has been focused on enzymes produced by cold-adapted micro-organisms. It has emerged that psychrophilic enzymes represent an extremely powerful tool in both protein folding investigations and for biotechnological purposes. Such enzymes are characterised by an increased thermosensitivity and, most of them, by a
D. Georlette   +12 more
openaire   +1 more source

Cold-adapted enzymes

Trends in Biotechnology, 1997
It is an article of faith among biochemists and molecular biologists that precious enzymes must be stored on ice. The usual reason given is that, at temperatures around freezing, enzyme activity is minimized and protein stability maximized. There is considerable evidence supporting this, but is it true for all enzymes? What about enzymes from organisms
openaire   +2 more sources

Cold Adaptation of the Thermophilic Enzyme 3-Isopropylmalate Dehydrogenase

Journal of Biochemistry, 2001
We have performed random mutagenesis coupled with selection to isolate mutant enzymes with high catalytic activities at low temperature from thermophilic 3-isopropylmalate dehydrogenase (IPMDH) originally isolated from Thermus thermophilus. Five cold-adapted mutant IPMDHs with single-amino-acid substitutions were obtained and analyzed. Kinetic analysis
M, Yasugi   +4 more
openaire   +2 more sources

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