Cell-free one-pot conversion of (+)-valencene to (+)-nootkatone by a unique dye-decolorizing peroxidase combined with a laccase from Funalia trogii
A combined system of a unique dye-decolorizing peroxidase (Ftr-DyP) and a laccase obtained from the basidiomycete Funalia trogii converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the pre...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2018-02, Vol.45 (2), p.89-101 |
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| creator | Kolwek, Julia Behrens, Christoph Linke, Diana Krings, Ulrich Berger, Ralf G. |
| description | A combined system of a unique dye-decolorizing peroxidase (Ftr-DyP) and a laccase obtained from the basidiomycete
Funalia trogii
converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the presence of 1 mM Mn
2+
and 2.5 mM
p
-coumaric acid, (+)-nootkatone was the predominating volatile product, and only traces of substrate and the nootkatols were detectable after 24 h. Hence, the two-enzyme-system reproduced the oxidizing activity observed before for the crude culture supernatant. The newly discovered Ftr-DyP was purified, sequenced and further characterized as a thermostable, non-glycosylated protein with a pH-optimum in the acidic range and a calculated mass of 52.3 kDa. Besides the typical activity of DyPs towards anthraquinone dyes, Ftr-DyP also oxidized Mn
2+
and showed activity in the absence of hydrogen peroxide. Neither the DyP from
Mycetinis scorodonius
nor the manganese peroxidase from
Nematoloma frowardii
were able to replace Ftr-DyP in this reaction. A hypothetical reaction mechanism is presented. |
| doi_str_mv | 10.1007/s10295-017-1998-9 |
| format | Article |
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Funalia trogii
converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the presence of 1 mM Mn
2+
and 2.5 mM
p
-coumaric acid, (+)-nootkatone was the predominating volatile product, and only traces of substrate and the nootkatols were detectable after 24 h. Hence, the two-enzyme-system reproduced the oxidizing activity observed before for the crude culture supernatant. The newly discovered Ftr-DyP was purified, sequenced and further characterized as a thermostable, non-glycosylated protein with a pH-optimum in the acidic range and a calculated mass of 52.3 kDa. Besides the typical activity of DyPs towards anthraquinone dyes, Ftr-DyP also oxidized Mn
2+
and showed activity in the absence of hydrogen peroxide. Neither the DyP from
Mycetinis scorodonius
nor the manganese peroxidase from
Nematoloma frowardii
were able to replace Ftr-DyP in this reaction. A hypothetical reaction mechanism is presented.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-017-1998-9</identifier><identifier>PMID: 29270883</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Anthraquinone ; Anthraquinone dyes ; Anthraquinones - metabolism ; Basidiomycota - enzymology ; Biocatalysis - Original Paper ; Biochemistry ; Bioinformatics ; Biomedical and Life Sciences ; Biotechnology ; Cell culture ; Chemical reactions ; Coloring Agents - metabolism ; Coumaric acid ; Decoloring ; Dyes ; Flavor ; Genetic Engineering ; Grapefruit ; Hydrogen peroxide ; Inorganic Chemistry ; Laccase ; Laccase - metabolism ; Life Sciences ; Manganese ; Manganese peroxidase ; Microbiology ; Oxidation ; Oxidation-Reduction ; p-Coumaric acid ; Peroxidase ; Peroxidase - metabolism ; pH effects ; Reaction mechanisms ; Sesquiterpenes - metabolism ; Substrates ; Valencene</subject><ispartof>Journal of industrial microbiology & biotechnology, 2018-02, Vol.45 (2), p.89-101</ispartof><rights>Society for Industrial Microbiology and Biotechnology 2017</rights><rights>Journal of Industrial Microbiology & Biotechnology is a copyright of Springer, (2017). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-9aa205da71c49faf41ad4fcf3b6e35839122bf69c42e34fe1a36c14f8e439b2a3</citedby><cites>FETCH-LOGICAL-c372t-9aa205da71c49faf41ad4fcf3b6e35839122bf69c42e34fe1a36c14f8e439b2a3</cites><orcidid>0000-0003-0477-2078</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/s10295-017-1998-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-017-1998-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27911,27912,41475,42544,51306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29270883$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kolwek, Julia</creatorcontrib><creatorcontrib>Behrens, Christoph</creatorcontrib><creatorcontrib>Linke, Diana</creatorcontrib><creatorcontrib>Krings, Ulrich</creatorcontrib><creatorcontrib>Berger, Ralf G.</creatorcontrib><title>Cell-free one-pot conversion of (+)-valencene to (+)-nootkatone by a unique dye-decolorizing peroxidase combined with a laccase from Funalia trogii</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>A combined system of a unique dye-decolorizing peroxidase (Ftr-DyP) and a laccase obtained from the basidiomycete
Funalia trogii
converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the presence of 1 mM Mn
2+
and 2.5 mM
p
-coumaric acid, (+)-nootkatone was the predominating volatile product, and only traces of substrate and the nootkatols were detectable after 24 h. Hence, the two-enzyme-system reproduced the oxidizing activity observed before for the crude culture supernatant. The newly discovered Ftr-DyP was purified, sequenced and further characterized as a thermostable, non-glycosylated protein with a pH-optimum in the acidic range and a calculated mass of 52.3 kDa. Besides the typical activity of DyPs towards anthraquinone dyes, Ftr-DyP also oxidized Mn
2+
and showed activity in the absence of hydrogen peroxide. Neither the DyP from
Mycetinis scorodonius
nor the manganese peroxidase from
Nematoloma frowardii
were able to replace Ftr-DyP in this reaction. A hypothetical reaction mechanism is presented.</description><subject>Anthraquinone</subject><subject>Anthraquinone dyes</subject><subject>Anthraquinones - metabolism</subject><subject>Basidiomycota - enzymology</subject><subject>Biocatalysis - Original Paper</subject><subject>Biochemistry</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cell culture</subject><subject>Chemical reactions</subject><subject>Coloring Agents - metabolism</subject><subject>Coumaric acid</subject><subject>Decoloring</subject><subject>Dyes</subject><subject>Flavor</subject><subject>Genetic Engineering</subject><subject>Grapefruit</subject><subject>Hydrogen peroxide</subject><subject>Inorganic Chemistry</subject><subject>Laccase</subject><subject>Laccase - metabolism</subject><subject>Life Sciences</subject><subject>Manganese</subject><subject>Manganese peroxidase</subject><subject>Microbiology</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>p-Coumaric acid</subject><subject>Peroxidase</subject><subject>Peroxidase - 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Academic</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kolwek, Julia</au><au>Behrens, Christoph</au><au>Linke, Diana</au><au>Krings, Ulrich</au><au>Berger, Ralf G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell-free one-pot conversion of (+)-valencene to (+)-nootkatone by a unique dye-decolorizing peroxidase combined with a laccase from Funalia trogii</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2018-02-01</date><risdate>2018</risdate><volume>45</volume><issue>2</issue><spage>89</spage><epage>101</epage><pages>89-101</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>A combined system of a unique dye-decolorizing peroxidase (Ftr-DyP) and a laccase obtained from the basidiomycete
Funalia trogii
converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the presence of 1 mM Mn
2+
and 2.5 mM
p
-coumaric acid, (+)-nootkatone was the predominating volatile product, and only traces of substrate and the nootkatols were detectable after 24 h. Hence, the two-enzyme-system reproduced the oxidizing activity observed before for the crude culture supernatant. The newly discovered Ftr-DyP was purified, sequenced and further characterized as a thermostable, non-glycosylated protein with a pH-optimum in the acidic range and a calculated mass of 52.3 kDa. Besides the typical activity of DyPs towards anthraquinone dyes, Ftr-DyP also oxidized Mn
2+
and showed activity in the absence of hydrogen peroxide. Neither the DyP from
Mycetinis scorodonius
nor the manganese peroxidase from
Nematoloma frowardii
were able to replace Ftr-DyP in this reaction. A hypothetical reaction mechanism is presented.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29270883</pmid><doi>10.1007/s10295-017-1998-9</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0003-0477-2078</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1367-5435 |
| ispartof | Journal of industrial microbiology & biotechnology, 2018-02, Vol.45 (2), p.89-101 |
| issn | 1367-5435 1476-5535 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1979967629 |
| source | MEDLINE; Oxford Journals Open Access Collection; Springer Nature - Complete Springer Journals |
| subjects | Anthraquinone Anthraquinone dyes Anthraquinones - metabolism Basidiomycota - enzymology Biocatalysis - Original Paper Biochemistry Bioinformatics Biomedical and Life Sciences Biotechnology Cell culture Chemical reactions Coloring Agents - metabolism Coumaric acid Decoloring Dyes Flavor Genetic Engineering Grapefruit Hydrogen peroxide Inorganic Chemistry Laccase Laccase - metabolism Life Sciences Manganese Manganese peroxidase Microbiology Oxidation Oxidation-Reduction p-Coumaric acid Peroxidase Peroxidase - metabolism pH effects Reaction mechanisms Sesquiterpenes - metabolism Substrates Valencene |
| title | Cell-free one-pot conversion of (+)-valencene to (+)-nootkatone by a unique dye-decolorizing peroxidase combined with a laccase from Funalia trogii |
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