Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature
Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins' sequence and structural organization that result in high confor...
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Language: | English |
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Online Access: | http://hdl.handle.net/10281/295731 https://doi.org/10.3390/md18110579 |
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ftunivmilanobic:oai:boa.unimib.it:10281/295731 2024-04-14T08:04:01+00:00 Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature Orlando, Marco Pucciarelli, Sandra Lotti, Marina Orlando, M Pucciarelli, S Lotti, M 2020 http://hdl.handle.net/10281/295731 https://doi.org/10.3390/md18110579 eng eng NLM (Medline) info:eu-repo/semantics/altIdentifier/pmid/33233712 info:eu-repo/semantics/altIdentifier/wos/WOS:000593426800001 volume:18 issue:11 journal:MARINE DRUGS http://hdl.handle.net/10281/295731 doi:10.3390/md18110579 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85096817023 cold adaptation cold-active enzyme endolysin glycoside hydrolase 19 info:eu-repo/semantics/article 2020 ftunivmilanobic https://doi.org/10.3390/md18110579 2024-03-21T17:19:31Z Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins' sequence and structural organization that result in high conformational flexibility. As a consequence of flexibility, several such enzymes are inherently heat sensitive. Cold-active enzymes are of interest for application in a number of bioprocesses, where cold activity coupled with easy thermal inactivation can be of advantage. We describe the biochemical and functional properties of two glycosyl hydrolases (named LYS177 and LYS188) of family 19 (GH19), identified in the genome of an Antarctic marine Pseudomonas. Molecular evolutionary analysis placed them in a group of characterized GH19 endolysins active on lysozyme substrates, such as peptidoglycan. Enzyme activity peaks at about 25-35 °C and 40% residual activity is retained at 5 °C. LYS177 and LYS188 are thermolabile, with Tm of 52 and 45 °C and half-lives of 48 and 12 h at 37 °C, respectively. Bioinformatics analyses suggest that low heat stability may be associated to temperature-driven increases in local flexibility occurring mainly in a specific region of the polypeptide that is predicted to contain hot spots for aggregation. Article in Journal/Newspaper Antarc* Antarctic Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive) Antarctic Marine Drugs 18 11 579 |
institution |
Open Polar |
collection |
Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive) |
op_collection_id |
ftunivmilanobic |
language |
English |
topic |
cold adaptation cold-active enzyme endolysin glycoside hydrolase 19 |
spellingShingle |
cold adaptation cold-active enzyme endolysin glycoside hydrolase 19 Orlando, Marco Pucciarelli, Sandra Lotti, Marina Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
topic_facet |
cold adaptation cold-active enzyme endolysin glycoside hydrolase 19 |
description |
Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins' sequence and structural organization that result in high conformational flexibility. As a consequence of flexibility, several such enzymes are inherently heat sensitive. Cold-active enzymes are of interest for application in a number of bioprocesses, where cold activity coupled with easy thermal inactivation can be of advantage. We describe the biochemical and functional properties of two glycosyl hydrolases (named LYS177 and LYS188) of family 19 (GH19), identified in the genome of an Antarctic marine Pseudomonas. Molecular evolutionary analysis placed them in a group of characterized GH19 endolysins active on lysozyme substrates, such as peptidoglycan. Enzyme activity peaks at about 25-35 °C and 40% residual activity is retained at 5 °C. LYS177 and LYS188 are thermolabile, with Tm of 52 and 45 °C and half-lives of 48 and 12 h at 37 °C, respectively. Bioinformatics analyses suggest that low heat stability may be associated to temperature-driven increases in local flexibility occurring mainly in a specific region of the polypeptide that is predicted to contain hot spots for aggregation. |
author2 |
Orlando, M Pucciarelli, S Lotti, M |
format |
Article in Journal/Newspaper |
author |
Orlando, Marco Pucciarelli, Sandra Lotti, Marina |
author_facet |
Orlando, Marco Pucciarelli, Sandra Lotti, Marina |
author_sort |
Orlando, Marco |
title |
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
title_short |
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
title_full |
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
title_fullStr |
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
title_full_unstemmed |
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature |
title_sort |
endolysins from antarctic pseudomonas display lysozyme activity at low temperature |
publisher |
NLM (Medline) |
publishDate |
2020 |
url |
http://hdl.handle.net/10281/295731 https://doi.org/10.3390/md18110579 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/33233712 info:eu-repo/semantics/altIdentifier/wos/WOS:000593426800001 volume:18 issue:11 journal:MARINE DRUGS http://hdl.handle.net/10281/295731 doi:10.3390/md18110579 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85096817023 |
op_doi |
https://doi.org/10.3390/md18110579 |
container_title |
Marine Drugs |
container_volume |
18 |
container_issue |
11 |
container_start_page |
579 |
_version_ |
1796300377679724544 |