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...
Published in: | Marine Drugs |
---|---|
Main Authors: | , , , , |
Format: | Text |
Language: | English |
Published: |
MDPI
2021
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912073/ http://www.ncbi.nlm.nih.gov/pubmed/33513970 https://doi.org/10.3390/md19020067 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:7912073 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:7912073 2023-05-15T13:48:31+02:00 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 2021-01-27 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912073/ http://www.ncbi.nlm.nih.gov/pubmed/33513970 https://doi.org/10.3390/md19020067 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912073/ http://www.ncbi.nlm.nih.gov/pubmed/33513970 http://dx.doi.org/10.3390/md19020067 © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Mar Drugs Article Text 2021 ftpubmed https://doi.org/10.3390/md19020067 2021-03-07T02:00:07Z 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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic Marine Drugs 19 2 67 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Article |
spellingShingle |
Article 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 |
topic_facet |
Article |
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. |
format |
Text |
author |
Yang, Guang Mozzicafreddo, Matteo Ballarini, Patrizia Pucciarelli, Sandra Miceli, Cristina |
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 |
publisher |
MDPI |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912073/ http://www.ncbi.nlm.nih.gov/pubmed/33513970 https://doi.org/10.3390/md19020067 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Mar Drugs |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912073/ http://www.ncbi.nlm.nih.gov/pubmed/33513970 http://dx.doi.org/10.3390/md19020067 |
op_rights |
© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.3390/md19020067 |
container_title |
Marine Drugs |
container_volume |
19 |
container_issue |
2 |
container_start_page |
67 |
_version_ |
1766249395315015680 |