Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production
Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate spe...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Miklaszewska, Magdalena [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2018 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 102(2018), 9 vom: 03. März, Seite 4063-4074 |
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| Übergeordnetes Werk: |
volume:102 ; year:2018 ; number:9 ; day:03 ; month:03 ; pages:4063-4074 |
| Links: |
|---|
| DOI / URN: |
10.1007/s00253-018-8878-8 |
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OLC2050792476 |
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| 520 | |a Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. | ||
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10.1007/s00253-018-8878-8 doi (DE-627)OLC2050792476 (DE-He213)s00253-018-8878-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Miklaszewska, Magdalena verfasserin (orcid)0000-0002-7108-4761 aut Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. Wax synthase Fatty acyl reductase Wax esters Fatty alcohols Dittrich-Domergue, Franziska aut Banaś, Antoni aut Domergue, Frédéric aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 9 vom: 03. März, Seite 4063-4074 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:9 day:03 month:03 pages:4063-4074 https://doi.org/10.1007/s00253-018-8878-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 9 03 03 4063-4074 |
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10.1007/s00253-018-8878-8 doi (DE-627)OLC2050792476 (DE-He213)s00253-018-8878-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Miklaszewska, Magdalena verfasserin (orcid)0000-0002-7108-4761 aut Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. Wax synthase Fatty acyl reductase Wax esters Fatty alcohols Dittrich-Domergue, Franziska aut Banaś, Antoni aut Domergue, Frédéric aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 9 vom: 03. März, Seite 4063-4074 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:9 day:03 month:03 pages:4063-4074 https://doi.org/10.1007/s00253-018-8878-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 9 03 03 4063-4074 |
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10.1007/s00253-018-8878-8 doi (DE-627)OLC2050792476 (DE-He213)s00253-018-8878-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Miklaszewska, Magdalena verfasserin (orcid)0000-0002-7108-4761 aut Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. Wax synthase Fatty acyl reductase Wax esters Fatty alcohols Dittrich-Domergue, Franziska aut Banaś, Antoni aut Domergue, Frédéric aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 9 vom: 03. März, Seite 4063-4074 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:9 day:03 month:03 pages:4063-4074 https://doi.org/10.1007/s00253-018-8878-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 9 03 03 4063-4074 |
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10.1007/s00253-018-8878-8 doi (DE-627)OLC2050792476 (DE-He213)s00253-018-8878-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Miklaszewska, Magdalena verfasserin (orcid)0000-0002-7108-4761 aut Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. Wax synthase Fatty acyl reductase Wax esters Fatty alcohols Dittrich-Domergue, Franziska aut Banaś, Antoni aut Domergue, Frédéric aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 9 vom: 03. März, Seite 4063-4074 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:9 day:03 month:03 pages:4063-4074 https://doi.org/10.1007/s00253-018-8878-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 9 03 03 4063-4074 |
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Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production |
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Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production |
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Miklaszewska, Magdalena |
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wax synthase mhws2 from marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production |
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Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production |
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Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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Abstract Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
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