An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation
Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of s...
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/471942 2024-04-14T08:02:13+00:00 An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina 2021 https://hdl.handle.net/11581/471942 https://doi.org/10.3390/md19020067 https://www.mdpi.com/1660-3397/19/2/67 eng eng info:eu-repo/semantics/altIdentifier/pmid/33513970 info:eu-repo/semantics/altIdentifier/wos/WOS:000622744000001 volume:19 issue:2 firstpage:1 lastpage:16 numberofpages:16 journal:MARINE DRUGS https://hdl.handle.net/11581/471942 doi:10.3390/md19020067 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85100627319 https://www.mdpi.com/1660-3397/19/2/67 info:eu-repo/semantics/openAccess info:eu-repo/semantics/article 2021 ftuncamerinoiris https://doi.org/10.3390/md19020067 2024-03-21T20:36:26Z Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic Euplotes focardii and the mesophilic Euplotes crassus. By applying bioinformatics approaches, we compared amino acid composition and predicted secondary and tertiary structures of these lipases to extract relevant information relative to cold adaptation. Our results not only confirm the importance of several previous recognized amino acid substitutions for cold adaptation, as the preference for small amino acid, but also identify some new factors correlated with the secondary structure possibly responsible for enhanced enzyme activity at low temperatures. This study emphasizes the subtle sequence and structural modifications that may help to transform mesophilic into psychrophilic enzymes for industrial applications by protein engineering. Article in Journal/Newspaper Antarc* Antarctic CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) Antarctic The Antarctic Marine Drugs 19 2 67 |
institution |
Open Polar |
collection |
CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
op_collection_id |
ftuncamerinoiris |
language |
English |
description |
Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic Euplotes focardii and the mesophilic Euplotes crassus. By applying bioinformatics approaches, we compared amino acid composition and predicted secondary and tertiary structures of these lipases to extract relevant information relative to cold adaptation. Our results not only confirm the importance of several previous recognized amino acid substitutions for cold adaptation, as the preference for small amino acid, but also identify some new factors correlated with the secondary structure possibly responsible for enhanced enzyme activity at low temperatures. This study emphasizes the subtle sequence and structural modifications that may help to transform mesophilic into psychrophilic enzymes for industrial applications by protein engineering. |
author2 |
Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina |
format |
Article in Journal/Newspaper |
author |
Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina |
spellingShingle |
Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
author_facet |
Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina |
author_sort |
Yang, Guang |
title |
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
title_short |
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
title_full |
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
title_fullStr |
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
title_full_unstemmed |
An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation |
title_sort |
in-silico comparative study of lipases from the antarctic psychrophilic ciliate euplotes focardii and the mesophilic congeneric species euplotes crassus: insight into molecular cold-adaptation |
publishDate |
2021 |
url |
https://hdl.handle.net/11581/471942 https://doi.org/10.3390/md19020067 https://www.mdpi.com/1660-3397/19/2/67 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/33513970 info:eu-repo/semantics/altIdentifier/wos/WOS:000622744000001 volume:19 issue:2 firstpage:1 lastpage:16 numberofpages:16 journal:MARINE DRUGS https://hdl.handle.net/11581/471942 doi:10.3390/md19020067 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85100627319 https://www.mdpi.com/1660-3397/19/2/67 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.3390/md19020067 |
container_title |
Marine Drugs |
container_volume |
19 |
container_issue |
2 |
container_start_page |
67 |
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1796313401015664640 |