Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis
The aminopeptidase gene from Mesorhizobium SEMIA3007 was cloned and overexpressed in Escherichia coli . The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 °C and was strongly activated by Co 2+ and Mn 2+ . Under these reaction conditions, the enzyme displayed K m and k cat values...
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| description | The aminopeptidase gene from
Mesorhizobium
SEMIA3007 was cloned and overexpressed in
Escherichia coli
. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 °C and was strongly activated by Co
2+
and Mn
2+
. Under these reaction conditions, the enzyme displayed K
m
and k
cat
values of 0.2364 ± 0.018 mM and 712.1 ± 88.12 s
−1
, respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism’s aminopeptidase activity. However, the enzyme’s absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from
Mesorhizobium
and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the
Mesorhizobium
genus and its importance in bacterial metabolism. |
| doi_str_mv | 10.1038/s41598-017-10932-8 |
| format | Article |
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Mesorhizobium
SEMIA3007 was cloned and overexpressed in
Escherichia coli
. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 °C and was strongly activated by Co
2+
and Mn
2+
. Under these reaction conditions, the enzyme displayed K
m
and k
cat
values of 0.2364 ± 0.018 mM and 712.1 ± 88.12 s
−1
, respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism’s aminopeptidase activity. However, the enzyme’s absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from
Mesorhizobium
and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the
Mesorhizobium
genus and its importance in bacterial metabolism.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-10932-8</identifier><identifier>PMID: 28878230</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>119/118 ; 13/44 ; 38/22 ; 38/39 ; 38/70 ; 45/23 ; 45/77 ; 631/326/2522 ; 631/45/607/468 ; 82/16 ; 82/29 ; 82/47 ; 82/80 ; 82/83 ; Aminopeptidase ; Biofilms ; Biotechnology ; Carbon dioxide ; Clean technology ; Cobalt ; E coli ; Enzymes ; Humanities and Social Sciences ; multidisciplinary ; Organic solvents ; Osmoregulation ; Osmotic stress ; pH effects ; Salinity tolerance ; Science ; Science (multidisciplinary) ; Sodium chloride ; Solvents</subject><ispartof>Scientific reports, 2017-09, Vol.7 (1), p.10684-14, Article 10684</ispartof><rights>The Author(s) 2017</rights><rights>2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-6b837ef6a990bc6a0a5a0dfa4c5f41c32323f914b90eba92ce3dc632a80d813b3</citedby><cites>FETCH-LOGICAL-c474t-6b837ef6a990bc6a0a5a0dfa4c5f41c32323f914b90eba92ce3dc632a80d813b3</cites><orcidid>0000-0003-4401-3869</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5587760/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5587760/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27903,27904,41099,42168,51554,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28878230$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sierra, Elwi Machado</creatorcontrib><creatorcontrib>Pereira, Mariana Rangel</creatorcontrib><creatorcontrib>Maester, Thaís Carvalho</creatorcontrib><creatorcontrib>Gomes-Pepe, Elisangela Soares</creatorcontrib><creatorcontrib>Mendoza, Elkin Rodas</creatorcontrib><creatorcontrib>Lemos, Eliana G. de Macedo</creatorcontrib><title>Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>The aminopeptidase gene from
Mesorhizobium
SEMIA3007 was cloned and overexpressed in
Escherichia coli
. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 °C and was strongly activated by Co
2+
and Mn
2+
. Under these reaction conditions, the enzyme displayed K
m
and k
cat
values of 0.2364 ± 0.018 mM and 712.1 ± 88.12 s
−1
, respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism’s aminopeptidase activity. However, the enzyme’s absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from
Mesorhizobium
and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the
Mesorhizobium
genus and its importance in bacterial metabolism.</description><subject>119/118</subject><subject>13/44</subject><subject>38/22</subject><subject>38/39</subject><subject>38/70</subject><subject>45/23</subject><subject>45/77</subject><subject>631/326/2522</subject><subject>631/45/607/468</subject><subject>82/16</subject><subject>82/29</subject><subject>82/47</subject><subject>82/80</subject><subject>82/83</subject><subject>Aminopeptidase</subject><subject>Biofilms</subject><subject>Biotechnology</subject><subject>Carbon dioxide</subject><subject>Clean technology</subject><subject>Cobalt</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Humanities and Social Sciences</subject><subject>multidisciplinary</subject><subject>Organic solvents</subject><subject>Osmoregulation</subject><subject>Osmotic stress</subject><subject>pH effects</subject><subject>Salinity tolerance</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sodium chloride</subject><subject>Solvents</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU1v1DAQhi0EolXpH-CALHHhkuKPJLYvSFVVaKWuOABna-I4G1eJHWynqNz453i7pVqQ8MVjzTPvzPhF6DUlZ5Rw-T7VtFGyIlRUlCjOKvkMHTNSNxXjjD0_iI_QaUq3pJyGqZqql-iISSkk4-QY_bqCKeQw2Qg-Y5idD4tdsushWbxhCg8xzHhjU4ij-xk6t874y-Xm-hxzQgT-4fKIOxeyNaMPU9g6AxNeyttnVyLwPXY5YTcvYDIOfgcPbppxuvd5tMmlV-jFAFOyp4_3Cfr28fLrxVV18_nT9cX5TWVqUeeq7SQXdmhBKdKZFgg0QPoBatMMNTW8bMoHRetOEduBYsby3rScgSS9pLzjJ-jDXndZu9n2pkwYYdJLdDPEex3A6b8z3o16G-5000ghWlIE3j0KxPB9tSnr2SVjpwm8DWvSVPG2ZbuvLejbf9DbsEZf1itUI0TdSMoKxfaUiSGlaIenYSjRO5P13mRdTNYPJmtZit4crvFU8sfSAvA9kErKb2086P1_2d9t-rSD</recordid><startdate>20170906</startdate><enddate>20170906</enddate><creator>Sierra, Elwi Machado</creator><creator>Pereira, Mariana Rangel</creator><creator>Maester, Thaís Carvalho</creator><creator>Gomes-Pepe, Elisangela Soares</creator><creator>Mendoza, Elkin Rodas</creator><creator>Lemos, Eliana G. de Macedo</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4401-3869</orcidid></search><sort><creationdate>20170906</creationdate><title>Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis</title><author>Sierra, Elwi Machado ; 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Mesorhizobium
SEMIA3007 was cloned and overexpressed in
Escherichia coli
. The enzyme called MesoAmp exhibited optimum activity at pH 8.5 and 45 °C and was strongly activated by Co
2+
and Mn
2+
. Under these reaction conditions, the enzyme displayed K
m
and k
cat
values of 0.2364 ± 0.018 mM and 712.1 ± 88.12 s
−1
, respectively. Additionally, the enzyme showed remarkable stability in organic solvents and was active at high concentrations of NaCl, suggesting that the enzyme might be suitable for use in biotechnology. MesoAmp is responsible for 40% of the organism’s aminopeptidase activity. However, the enzyme’s absence does not affect bacterial growth in synthetic broth, although it interfered with biofilm synthesis and osmoregulation. To the best of our knowledge, this report describes the first detailed characterization of aminopeptidase from
Mesorhizobium
and suggests its importance in biofilm formation and osmotic stress tolerance. In summary, this work lays the foundation for potential biotechnological applications and/or the development of environmentally friendly technologies and describes the first solvent- and halo-tolerant aminopeptidases identified from the
Mesorhizobium
genus and its importance in bacterial metabolism.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28878230</pmid><doi>10.1038/s41598-017-10932-8</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0003-4401-3869</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 119/118 13/44 38/22 38/39 38/70 45/23 45/77 631/326/2522 631/45/607/468 82/16 82/29 82/47 82/80 82/83 Aminopeptidase Biofilms Biotechnology Carbon dioxide Clean technology Cobalt E coli Enzymes Humanities and Social Sciences multidisciplinary Organic solvents Osmoregulation Osmotic stress pH effects Salinity tolerance Science Science (multidisciplinary) Sodium chloride Solvents |
| title | Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis |
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