Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens
The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of Pseudomonas strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in E. coli . Th...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2018-07, Vol.102 (14), p.6057-6068 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Schmidt, Nina G. Żądło-Dobrowolska, Anna Ruppert, Valerie Höflehner, Christian Wiltschi, Birgit Kroutil, Wolfgang |
| description | The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of
Pseudomonas
strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in
E. coli
. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. Moreover, the impact of bivalent metals, inhibitors, and other additives was tested. Careful selection of expression and working conditions led to obtain recombinant acyltransferase form
Pseudomonas protegens
with up to 11 U mL
−1
activity. |
| doi_str_mv | 10.1007/s00253-018-9052-z |
| format | Article |
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Pseudomonas
strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in
E. coli
. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. Moreover, the impact of bivalent metals, inhibitors, and other additives was tested. Careful selection of expression and working conditions led to obtain recombinant acyltransferase form
Pseudomonas protegens
with up to 11 U mL
−1
activity.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-018-9052-z</identifier><identifier>PMID: 29754162</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Acyltransferase ; acyltransferases ; Acyltransferases - genetics ; Additives ; Amino Acid Sequence ; Bacterial Proteins - genetics ; Biomedical and Life Sciences ; Biosynthetic Pathways ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; chemical bonding ; Cloning ; Cloning, Molecular ; E coli ; enzyme activity ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene expression ; Genetic aspects ; heterologous gene expression ; Identification methods ; Life Sciences ; Metals ; Microbial Genetics and Genomics ; Microbiological research ; Microbiology ; Molecular chains ; molecular cloning ; Operon ; Physiological aspects ; Pseudomonas ; Pseudomonas - enzymology ; Pseudomonas - genetics ; Pseudomonas protegens ; Shelf life ; storage quality ; Storage stability ; Transferases ; Working conditions</subject><ispartof>Applied microbiology and biotechnology, 2018-07, Vol.102 (14), p.6057-6068</ispartof><rights>The Author(s) 2018</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c568t-7419f0e37753ccf7530a793cf796d292379e99a42a2d68e7a1cb27129d9bbd1a3</citedby><cites>FETCH-LOGICAL-c568t-7419f0e37753ccf7530a793cf796d292379e99a42a2d68e7a1cb27129d9bbd1a3</cites><orcidid>0000-0002-2151-6394</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-018-9052-z$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-018-9052-z$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29754162$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schmidt, Nina G.</creatorcontrib><creatorcontrib>Żądło-Dobrowolska, Anna</creatorcontrib><creatorcontrib>Ruppert, Valerie</creatorcontrib><creatorcontrib>Höflehner, Christian</creatorcontrib><creatorcontrib>Wiltschi, Birgit</creatorcontrib><creatorcontrib>Kroutil, Wolfgang</creatorcontrib><title>Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of
Pseudomonas
strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in
E. coli
. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. Moreover, the impact of bivalent metals, inhibitors, and other additives was tested. Careful selection of expression and working conditions led to obtain recombinant acyltransferase form
Pseudomonas protegens
with up to 11 U mL
−1
activity.</description><subject>Acyltransferase</subject><subject>acyltransferases</subject><subject>Acyltransferases - genetics</subject><subject>Additives</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - genetics</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthetic Pathways</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>chemical bonding</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>enzyme activity</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>heterologous gene expression</subject><subject>Identification methods</subject><subject>Life Sciences</subject><subject>Metals</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiological research</subject><subject>Microbiology</subject><subject>Molecular chains</subject><subject>molecular cloning</subject><subject>Operon</subject><subject>Physiological aspects</subject><subject>Pseudomonas</subject><subject>Pseudomonas - enzymology</subject><subject>Pseudomonas - genetics</subject><subject>Pseudomonas protegens</subject><subject>Shelf life</subject><subject>storage quality</subject><subject>Storage stability</subject><subject>Transferases</subject><subject>Working conditions</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkk9v1DAQxS0EokvhA3BBkbhwaMD_HV-QqooCUhEc4GzNOpM0VWIvdoLofvp6ldICEuIytjy_eXoePUKeM_qaUWreZEq5EjVlTW2p4vX-AdkwKXhNNZMPyYYyo2qjbHNEnuR8RSnjjdaPyRG3Rkmm-YbApziiX0ZIlR9jGEJ_UuHPXcKchxhOKght5S8hgZ8xDXuYy2sVuwr89TgnCLnDBBmrLsWp-pJxaeMUA-Rql-KMPYb8lDzqYMz47PY8Jt_O3309-1BffH7_8ez0ovZKN3NtJLMdRWGMEt53pVIwVpSb1S23XBiL1oLkwFvdoAHmt9wwblu73bYMxDF5u-rulu2ErcdQ_I1ul4YJ0rWLMLg_O2G4dH384TRlQnFZBF7dCqT4fcE8u2nIHscRAsYlO85WUNn_o1Q0hppSC_ryL_QqLimUTRwo0yhhlLmnehjRDaGLxaI_iLpTJYUVUmpaKLZSPsWcE3Z3v2PUHRLh1kS4kgh3SITbl5kXv6_lbuJXBArAVyCXVugx3Rv8t-oNoKrB_g</recordid><startdate>20180701</startdate><enddate>20180701</enddate><creator>Schmidt, Nina G.</creator><creator>Żądło-Dobrowolska, Anna</creator><creator>Ruppert, Valerie</creator><creator>Höflehner, Christian</creator><creator>Wiltschi, Birgit</creator><creator>Kroutil, Wolfgang</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2151-6394</orcidid></search><sort><creationdate>20180701</creationdate><title>Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens</title><author>Schmidt, Nina G. ; Żądło-Dobrowolska, Anna ; Ruppert, Valerie ; Höflehner, Christian ; Wiltschi, Birgit ; Kroutil, Wolfgang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c568t-7419f0e37753ccf7530a793cf796d292379e99a42a2d68e7a1cb27129d9bbd1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Acyltransferase</topic><topic>acyltransferases</topic><topic>Acyltransferases - genetics</topic><topic>Additives</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - genetics</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthetic Pathways</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>chemical bonding</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>E coli</topic><topic>enzyme activity</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>heterologous gene expression</topic><topic>Identification methods</topic><topic>Life Sciences</topic><topic>Metals</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiological research</topic><topic>Microbiology</topic><topic>Molecular chains</topic><topic>molecular cloning</topic><topic>Operon</topic><topic>Physiological aspects</topic><topic>Pseudomonas</topic><topic>Pseudomonas - enzymology</topic><topic>Pseudomonas - genetics</topic><topic>Pseudomonas protegens</topic><topic>Shelf life</topic><topic>storage quality</topic><topic>Storage stability</topic><topic>Transferases</topic><topic>Working conditions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schmidt, Nina G.</creatorcontrib><creatorcontrib>Żądło-Dobrowolska, Anna</creatorcontrib><creatorcontrib>Ruppert, Valerie</creatorcontrib><creatorcontrib>Höflehner, Christian</creatorcontrib><creatorcontrib>Wiltschi, Birgit</creatorcontrib><creatorcontrib>Kroutil, Wolfgang</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schmidt, Nina G.</au><au>Żądło-Dobrowolska, Anna</au><au>Ruppert, Valerie</au><au>Höflehner, Christian</au><au>Wiltschi, Birgit</au><au>Kroutil, Wolfgang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2018-07-01</date><risdate>2018</risdate><volume>102</volume><issue>14</issue><spage>6057</spage><epage>6068</epage><pages>6057-6068</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>The formation of C-C bonds by using CoA independent acyltransferases may have significant impact for novel methods for biotechnology. We report the identification of
Pseudomonas
strains with CoA-independent acyltransferase activity as well as the heterologous expression of the enzyme in
E. coli
. The cloning strategies and selected expression studies are discussed. The recombinant acyltransferases were characterized with regard to thermal and storage stability, pH,- and co-solvent tolerance. Moreover, the impact of bivalent metals, inhibitors, and other additives was tested. Careful selection of expression and working conditions led to obtain recombinant acyltransferase form
Pseudomonas protegens
with up to 11 U mL
−1
activity.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29754162</pmid><doi>10.1007/s00253-018-9052-z</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-2151-6394</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Applied microbiology and biotechnology, 2018-07, Vol.102 (14), p.6057-6068 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6013524 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Acyltransferase acyltransferases Acyltransferases - genetics Additives Amino Acid Sequence Bacterial Proteins - genetics Biomedical and Life Sciences Biosynthetic Pathways Biotechnologically Relevant Enzymes and Proteins Biotechnology chemical bonding Cloning Cloning, Molecular E coli enzyme activity Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Gene expression Genetic aspects heterologous gene expression Identification methods Life Sciences Metals Microbial Genetics and Genomics Microbiological research Microbiology Molecular chains molecular cloning Operon Physiological aspects Pseudomonas Pseudomonas - enzymology Pseudomonas - genetics Pseudomonas protegens Shelf life storage quality Storage stability Transferases Working conditions |
| title | Molecular cloning, expression, and characterization of acyltransferase from Pseudomonas protegens |
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