Enzymes from psychrophilic organisms
Psychrophilic organisms such as micro-organisms and other ectothermic species living in polar, deep- sea or any constantly low temperature environments, produce enzymes adapted to function at low temperature. These enzymes are characterized by a high catalytic efficiency at low and moderate temperat...
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fthighwire:oai:open-archive.highwire.org:femsre:18/2-3/189 2023-05-15T13:49:27+02:00 Enzymes from psychrophilic organisms Feller, Georges Narinx, Emmanuel Arpigny, Jean Louis Aittaleb, Mohamed Baise, Etienne Genicot, Sabine Gerday, Charles 1996-05-01 00:00:00.0 text/html http://femsre.oxfordjournals.org/cgi/content/short/18/2-3/189 https://doi.org/10.1111/j.1574-6976.1996.tb00236.x en eng Oxford University Press http://femsre.oxfordjournals.org/cgi/content/short/18/2-3/189 http://dx.doi.org/10.1111/j.1574-6976.1996.tb00236.x Copyright (C) 1996, Oxford University Press Articles TEXT 1996 fthighwire https://doi.org/10.1111/j.1574-6976.1996.tb00236.x 2016-11-16T18:18:11Z Psychrophilic organisms such as micro-organisms and other ectothermic species living in polar, deep- sea or any constantly low temperature environments, produce enzymes adapted to function at low temperature. These enzymes are characterized by a high catalytic efficiency at low and moderate temperatures but are rather thermolabile. Due to their high specific activity and their rapid inactivation at temperatures as low as 30°C, they offer, along with the producing micro-organisms, a great potential in biotechnology. The molecular basis of the adaptation of cold α-amylase, subtilisin, triose phosphate isomerase from Antarctic bacteria and of trypsin from fish living in North Atlantic and in Antarctic sea waters have been studied. The comparison of the 3D structures obtained either by protein modelling or by X-ray crystallography (North Atlantic trypsin) with those of their mesophilic counterparts indicates that the molecular changes tend to increase the flexibility of the structure by a weakening of the intramolecular interactions and by an increase of the interactions with the solvent. For each enzyme, the most appropriate strategy enabling it to accommodate the substrate at a low energy cost is selected. There is a price to pay in terms of thermosensibility because the selective pressure is essentially oriented towards the harmonization of the specific activity with ambient thermal conditions. However, as demonstrated by site-directed mutagenesis experiments carried out on the Antarctic subtilisin, the possibility remains to stabilize the structure of these enzymes without affecting their high catalytic efficiency. Text Antarc* Antarctic North Atlantic HighWire Press (Stanford University) Antarctic The Antarctic FEMS Microbiology Reviews 18 2-3 189 202 |
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Articles |
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Articles Feller, Georges Narinx, Emmanuel Arpigny, Jean Louis Aittaleb, Mohamed Baise, Etienne Genicot, Sabine Gerday, Charles Enzymes from psychrophilic organisms |
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description |
Psychrophilic organisms such as micro-organisms and other ectothermic species living in polar, deep- sea or any constantly low temperature environments, produce enzymes adapted to function at low temperature. These enzymes are characterized by a high catalytic efficiency at low and moderate temperatures but are rather thermolabile. Due to their high specific activity and their rapid inactivation at temperatures as low as 30°C, they offer, along with the producing micro-organisms, a great potential in biotechnology. The molecular basis of the adaptation of cold α-amylase, subtilisin, triose phosphate isomerase from Antarctic bacteria and of trypsin from fish living in North Atlantic and in Antarctic sea waters have been studied. The comparison of the 3D structures obtained either by protein modelling or by X-ray crystallography (North Atlantic trypsin) with those of their mesophilic counterparts indicates that the molecular changes tend to increase the flexibility of the structure by a weakening of the intramolecular interactions and by an increase of the interactions with the solvent. For each enzyme, the most appropriate strategy enabling it to accommodate the substrate at a low energy cost is selected. There is a price to pay in terms of thermosensibility because the selective pressure is essentially oriented towards the harmonization of the specific activity with ambient thermal conditions. However, as demonstrated by site-directed mutagenesis experiments carried out on the Antarctic subtilisin, the possibility remains to stabilize the structure of these enzymes without affecting their high catalytic efficiency. |
format |
Text |
author |
Feller, Georges Narinx, Emmanuel Arpigny, Jean Louis Aittaleb, Mohamed Baise, Etienne Genicot, Sabine Gerday, Charles |
author_facet |
Feller, Georges Narinx, Emmanuel Arpigny, Jean Louis Aittaleb, Mohamed Baise, Etienne Genicot, Sabine Gerday, Charles |
author_sort |
Feller, Georges |
title |
Enzymes from psychrophilic organisms |
title_short |
Enzymes from psychrophilic organisms |
title_full |
Enzymes from psychrophilic organisms |
title_fullStr |
Enzymes from psychrophilic organisms |
title_full_unstemmed |
Enzymes from psychrophilic organisms |
title_sort |
enzymes from psychrophilic organisms |
publisher |
Oxford University Press |
publishDate |
1996 |
url |
http://femsre.oxfordjournals.org/cgi/content/short/18/2-3/189 https://doi.org/10.1111/j.1574-6976.1996.tb00236.x |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic North Atlantic |
genre_facet |
Antarc* Antarctic North Atlantic |
op_relation |
http://femsre.oxfordjournals.org/cgi/content/short/18/2-3/189 http://dx.doi.org/10.1111/j.1574-6976.1996.tb00236.x |
op_rights |
Copyright (C) 1996, Oxford University Press |
op_doi |
https://doi.org/10.1111/j.1574-6976.1996.tb00236.x |
container_title |
FEMS Microbiology Reviews |
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18 |
container_issue |
2-3 |
container_start_page |
189 |
op_container_end_page |
202 |
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1766251388453519360 |