Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1
An esterase gene, estA1, was cloned from Alteromonas sp. 39-G1 isolated from the Beaufort Sea. The gene is composed of 1,140 nucleotides and codes for a 41,190 Da protein containing 379 amino acids. As a result of a BLAST search, the protein sequence of esterase EstA1 was found to be identical to Al...
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ftpubmed:oai:pubmedcentral.nih.gov:9728341 2023-05-15T15:40:37+02:00 Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 Won, Seok-Jae Jeong, Han Byeol Kim, Hyung-Kwoun 2020-02-28 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728341/ http://www.ncbi.nlm.nih.gov/pubmed/31838795 https://doi.org/10.4014/jmb.1907.07057 en eng Korean Society for Microbiology and Biotechnology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728341/ http://www.ncbi.nlm.nih.gov/pubmed/31838795 http://dx.doi.org/10.4014/jmb.1907.07057 Copyright©2020 by The Korean Society for Microbiology and Biotechnology https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/) . CC-BY J Microbiol Biotechnol Research article Text 2020 ftpubmed https://doi.org/10.4014/jmb.1907.07057 2022-12-18T01:35:03Z An esterase gene, estA1, was cloned from Alteromonas sp. 39-G1 isolated from the Beaufort Sea. The gene is composed of 1,140 nucleotides and codes for a 41,190 Da protein containing 379 amino acids. As a result of a BLAST search, the protein sequence of esterase EstA1 was found to be identical to Alteromonas sp. esterase (GenBank: PHS53692). As far as we know, no research on this enzyme has yet been conducted. Phylogenetic analysis showed that esterase EstA1 was a member of the bacterial lipolytic enzyme family IV (hormone sensitive lipases). Two deletion mutants (Δ20 and Δ54) of the esterase EstA1 were produced in Escherichia coli BL21 (DE3) cells with part of the N-terminal of the protein removed and His-tag attached to the C-terminal. These enzymes exhibited the highest activity toward p-nitrophenyl (pNP) acetate (C(2)) and had little or no activity towards pNP-esters with acyl chains longer than C6. Their optimum temperature and pH of the catalytic activity were 45°C and pH 8.0, respectively. As the NaCl concentration increased, their enzyme activities continued to increase and the highest enzyme activities were measured in 5 M NaCl. These enzymes were found to be stable for up to 8 h in the concentration of 3-5 M NaCl. Moreover, they have been found to be stable for various metal ions, detergents and organic solvents. These salt-tolerant and chemical-resistant properties suggest that the enzyme esterase EstA1 is both academically and industrially useful. Text Beaufort Sea PubMed Central (PMC) Journal of Microbiology and Biotechnology 30 2 216 225 |
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Research article Won, Seok-Jae Jeong, Han Byeol Kim, Hyung-Kwoun Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
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Research article |
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An esterase gene, estA1, was cloned from Alteromonas sp. 39-G1 isolated from the Beaufort Sea. The gene is composed of 1,140 nucleotides and codes for a 41,190 Da protein containing 379 amino acids. As a result of a BLAST search, the protein sequence of esterase EstA1 was found to be identical to Alteromonas sp. esterase (GenBank: PHS53692). As far as we know, no research on this enzyme has yet been conducted. Phylogenetic analysis showed that esterase EstA1 was a member of the bacterial lipolytic enzyme family IV (hormone sensitive lipases). Two deletion mutants (Δ20 and Δ54) of the esterase EstA1 were produced in Escherichia coli BL21 (DE3) cells with part of the N-terminal of the protein removed and His-tag attached to the C-terminal. These enzymes exhibited the highest activity toward p-nitrophenyl (pNP) acetate (C(2)) and had little or no activity towards pNP-esters with acyl chains longer than C6. Their optimum temperature and pH of the catalytic activity were 45°C and pH 8.0, respectively. As the NaCl concentration increased, their enzyme activities continued to increase and the highest enzyme activities were measured in 5 M NaCl. These enzymes were found to be stable for up to 8 h in the concentration of 3-5 M NaCl. Moreover, they have been found to be stable for various metal ions, detergents and organic solvents. These salt-tolerant and chemical-resistant properties suggest that the enzyme esterase EstA1 is both academically and industrially useful. |
format |
Text |
author |
Won, Seok-Jae Jeong, Han Byeol Kim, Hyung-Kwoun |
author_facet |
Won, Seok-Jae Jeong, Han Byeol Kim, Hyung-Kwoun |
author_sort |
Won, Seok-Jae |
title |
Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
title_short |
Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
title_full |
Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
title_fullStr |
Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
title_full_unstemmed |
Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine Bacterium Alteromonas sp. 39-G1 |
title_sort |
characterization of novel salt-tolerant esterase isolated from the marine bacterium alteromonas sp. 39-g1 |
publisher |
Korean Society for Microbiology and Biotechnology |
publishDate |
2020 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728341/ http://www.ncbi.nlm.nih.gov/pubmed/31838795 https://doi.org/10.4014/jmb.1907.07057 |
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Beaufort Sea |
genre_facet |
Beaufort Sea |
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J Microbiol Biotechnol |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9728341/ http://www.ncbi.nlm.nih.gov/pubmed/31838795 http://dx.doi.org/10.4014/jmb.1907.07057 |
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Copyright©2020 by The Korean Society for Microbiology and Biotechnology https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/) . |
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CC-BY |
op_doi |
https://doi.org/10.4014/jmb.1907.07057 |
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Journal of Microbiology and Biotechnology |
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30 |
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2 |
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216 |
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225 |
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1766373252671733760 |