Enzymes from psychrophilic organisms
peer reviewed 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 mod...
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Blackwell Publishing
1996
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Online Access: | https://orbi.uliege.be/handle/2268/17417 https://doi.org/10.1111/j.1574-6976.1996.tb00236.x |
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ftorbi:oai:orbi.ulg.ac.be:2268/17417 2024-04-21T07:46:24+00:00 Enzymes from psychrophilic organisms Feller, Georges Narinx, E. Arpigny, J. L. Aittaleb, M. Baise, Etienne Genicot, S. Gerday, Charles 1996 https://orbi.uliege.be/handle/2268/17417 https://doi.org/10.1111/j.1574-6976.1996.tb00236.x en eng Blackwell Publishing urn:issn:0168-6445 urn:issn:1574-6976 https://orbi.uliege.be/handle/2268/17417 info:hdl:2268/17417 doi:10.1111/j.1574-6976.1996.tb00236.x scopus-id:2-s2.0-0029883360 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess FEMS Microbiology Reviews, 18 (2-3), 189-202 (1996) cold enzyme psychrophile Antarctic bacterium adaptation to cold PROTEIN STABILITY NUCLEOTIDE-SEQUENCE ANTARCTIC BACTERIA HISTIDINE-RESIDUES MORAXELLA TA144 ALPHA-AMYLASE SUBTILISIN CLONING LIPASE TEMPERATURE Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 1996 ftorbi https://doi.org/10.1111/j.1574-6976.1996.tb00236.x 2024-03-27T14:59:09Z peer reviewed 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 degrees C, they offer, along with the producing micro-organisms, a great potential in biotechnology. The molecular basis of the adaptation of cold cu-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. Article in Journal/Newspaper Antarc* Antarctic North Atlantic University of Liège: ORBi (Open Repository and Bibliography) FEMS Microbiology Reviews 18 2-3 189 202 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
cold enzyme psychrophile Antarctic bacterium adaptation to cold PROTEIN STABILITY NUCLEOTIDE-SEQUENCE ANTARCTIC BACTERIA HISTIDINE-RESIDUES MORAXELLA TA144 ALPHA-AMYLASE SUBTILISIN CLONING LIPASE TEMPERATURE Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
cold enzyme psychrophile Antarctic bacterium adaptation to cold PROTEIN STABILITY NUCLEOTIDE-SEQUENCE ANTARCTIC BACTERIA HISTIDINE-RESIDUES MORAXELLA TA144 ALPHA-AMYLASE SUBTILISIN CLONING LIPASE TEMPERATURE Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Feller, Georges Narinx, E. Arpigny, J. L. Aittaleb, M. Baise, Etienne Genicot, S. Gerday, Charles Enzymes from psychrophilic organisms |
topic_facet |
cold enzyme psychrophile Antarctic bacterium adaptation to cold PROTEIN STABILITY NUCLEOTIDE-SEQUENCE ANTARCTIC BACTERIA HISTIDINE-RESIDUES MORAXELLA TA144 ALPHA-AMYLASE SUBTILISIN CLONING LIPASE TEMPERATURE Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed 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 degrees C, they offer, along with the producing micro-organisms, a great potential in biotechnology. The molecular basis of the adaptation of cold cu-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 |
Article in Journal/Newspaper |
author |
Feller, Georges Narinx, E. Arpigny, J. L. Aittaleb, M. Baise, Etienne Genicot, S. Gerday, Charles |
author_facet |
Feller, Georges Narinx, E. Arpigny, J. L. Aittaleb, M. Baise, Etienne Genicot, S. 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 |
Blackwell Publishing |
publishDate |
1996 |
url |
https://orbi.uliege.be/handle/2268/17417 https://doi.org/10.1111/j.1574-6976.1996.tb00236.x |
genre |
Antarc* Antarctic North Atlantic |
genre_facet |
Antarc* Antarctic North Atlantic |
op_source |
FEMS Microbiology Reviews, 18 (2-3), 189-202 (1996) |
op_relation |
urn:issn:0168-6445 urn:issn:1574-6976 https://orbi.uliege.be/handle/2268/17417 info:hdl:2268/17417 doi:10.1111/j.1574-6976.1996.tb00236.x scopus-id:2-s2.0-0029883360 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1111/j.1574-6976.1996.tb00236.x |
container_title |
FEMS Microbiology Reviews |
container_volume |
18 |
container_issue |
2-3 |
container_start_page |
189 |
op_container_end_page |
202 |
_version_ |
1796943395339370496 |