Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents
Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by meth...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Ribitsch, Doris [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2010 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2010 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 87(2010), 5 vom: 14. Mai, Seite 1743-1752 |
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| Übergeordnetes Werk: |
volume:87 ; year:2010 ; number:5 ; day:14 ; month:05 ; pages:1743-1752 |
| Links: |
|---|
| DOI / URN: |
10.1007/s00253-010-2637-9 |
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OLC2050730241 |
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| 520 | |a Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. | ||
| 650 | 4 | |a Choline oxidase | |
| 650 | 4 | |a Directed evolution | |
| 650 | 4 | |a Biological bleaching | |
| 650 | 4 | |a Detergents | |
| 650 | 4 | |a Hydrogen peroxide | |
| 700 | 1 | |a Winkler, Sonja |4 aut | |
| 700 | 1 | |a Gruber, Karl |4 aut | |
| 700 | 1 | |a Karl, Wolfgang |4 aut | |
| 700 | 1 | |a Wehrschütz-Sigl, Eva |4 aut | |
| 700 | 1 | |a Eiteljörg, Inge |4 aut | |
| 700 | 1 | |a Schratl, Petra |4 aut | |
| 700 | 1 | |a Remler, Peter |4 aut | |
| 700 | 1 | |a Stehr, Regina |4 aut | |
| 700 | 1 | |a Bessler, Cornelius |4 aut | |
| 700 | 1 | |a Mußmann, Nina |4 aut | |
| 700 | 1 | |a Sauter, Kerstin |4 aut | |
| 700 | 1 | |a Maurer, Karl Heinz |4 aut | |
| 700 | 1 | |a Schwab, Helmut |4 aut | |
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10.1007/s00253-010-2637-9 doi (DE-627)OLC2050730241 (DE-He213)s00253-010-2637-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ribitsch, Doris verfasserin aut Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2010 Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide Winkler, Sonja aut Gruber, Karl aut Karl, Wolfgang aut Wehrschütz-Sigl, Eva aut Eiteljörg, Inge aut Schratl, Petra aut Remler, Peter aut Stehr, Regina aut Bessler, Cornelius aut Mußmann, Nina aut Sauter, Kerstin aut Maurer, Karl Heinz aut Schwab, Helmut aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 87(2010), 5 vom: 14. Mai, Seite 1743-1752 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 https://doi.org/10.1007/s00253-010-2637-9 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_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 87 2010 5 14 05 1743-1752 |
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10.1007/s00253-010-2637-9 doi (DE-627)OLC2050730241 (DE-He213)s00253-010-2637-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ribitsch, Doris verfasserin aut Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2010 Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide Winkler, Sonja aut Gruber, Karl aut Karl, Wolfgang aut Wehrschütz-Sigl, Eva aut Eiteljörg, Inge aut Schratl, Petra aut Remler, Peter aut Stehr, Regina aut Bessler, Cornelius aut Mußmann, Nina aut Sauter, Kerstin aut Maurer, Karl Heinz aut Schwab, Helmut aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 87(2010), 5 vom: 14. Mai, Seite 1743-1752 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 https://doi.org/10.1007/s00253-010-2637-9 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_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 87 2010 5 14 05 1743-1752 |
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10.1007/s00253-010-2637-9 doi (DE-627)OLC2050730241 (DE-He213)s00253-010-2637-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ribitsch, Doris verfasserin aut Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2010 Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide Winkler, Sonja aut Gruber, Karl aut Karl, Wolfgang aut Wehrschütz-Sigl, Eva aut Eiteljörg, Inge aut Schratl, Petra aut Remler, Peter aut Stehr, Regina aut Bessler, Cornelius aut Mußmann, Nina aut Sauter, Kerstin aut Maurer, Karl Heinz aut Schwab, Helmut aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 87(2010), 5 vom: 14. Mai, Seite 1743-1752 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 https://doi.org/10.1007/s00253-010-2637-9 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_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 87 2010 5 14 05 1743-1752 |
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10.1007/s00253-010-2637-9 doi (DE-627)OLC2050730241 (DE-He213)s00253-010-2637-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ribitsch, Doris verfasserin aut Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2010 Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide Winkler, Sonja aut Gruber, Karl aut Karl, Wolfgang aut Wehrschütz-Sigl, Eva aut Eiteljörg, Inge aut Schratl, Petra aut Remler, Peter aut Stehr, Regina aut Bessler, Cornelius aut Mußmann, Nina aut Sauter, Kerstin aut Maurer, Karl Heinz aut Schwab, Helmut aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 87(2010), 5 vom: 14. Mai, Seite 1743-1752 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 https://doi.org/10.1007/s00253-010-2637-9 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_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 87 2010 5 14 05 1743-1752 |
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10.1007/s00253-010-2637-9 doi (DE-627)OLC2050730241 (DE-He213)s00253-010-2637-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Ribitsch, Doris verfasserin aut Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2010 Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide Winkler, Sonja aut Gruber, Karl aut Karl, Wolfgang aut Wehrschütz-Sigl, Eva aut Eiteljörg, Inge aut Schratl, Petra aut Remler, Peter aut Stehr, Regina aut Bessler, Cornelius aut Mußmann, Nina aut Sauter, Kerstin aut Maurer, Karl Heinz aut Schwab, Helmut aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 87(2010), 5 vom: 14. Mai, Seite 1743-1752 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 https://doi.org/10.1007/s00253-010-2637-9 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_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 87 2010 5 14 05 1743-1752 |
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Enthalten in Applied microbiology and biotechnology 87(2010), 5 vom: 14. Mai, Seite 1743-1752 volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 |
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Enthalten in Applied microbiology and biotechnology 87(2010), 5 vom: 14. Mai, Seite 1743-1752 volume:87 year:2010 number:5 day:14 month:05 pages:1743-1752 |
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Choline oxidase Directed evolution Biological bleaching Detergents Hydrogen peroxide |
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Ribitsch, Doris @@aut@@ Winkler, Sonja @@aut@@ Gruber, Karl @@aut@@ Karl, Wolfgang @@aut@@ Wehrschütz-Sigl, Eva @@aut@@ Eiteljörg, Inge @@aut@@ Schratl, Petra @@aut@@ Remler, Peter @@aut@@ Stehr, Regina @@aut@@ Bessler, Cornelius @@aut@@ Mußmann, Nina @@aut@@ Sauter, Kerstin @@aut@@ Maurer, Karl Heinz @@aut@@ Schwab, Helmut @@aut@@ |
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Ribitsch, Doris Winkler, Sonja Gruber, Karl Karl, Wolfgang Wehrschütz-Sigl, Eva Eiteljörg, Inge Schratl, Petra Remler, Peter Stehr, Regina Bessler, Cornelius Mußmann, Nina Sauter, Kerstin Maurer, Karl Heinz Schwab, Helmut |
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engineering of choline oxidase from arthrobacter nicotianae for potential use as biological bleach in detergents |
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Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents |
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Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. © Springer-Verlag 2010 |
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Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. © Springer-Verlag 2010 |
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Abstract In order to engineer the choline oxidase from Arthrobacter nicotianae (An_CodA) for the potential application as biological bleach in detergents, the specific activity of the enzyme toward the synthetic substrate tris-(2-hydroxyethyl)-methylammonium methylsulfate (MTEA) was improved by methods of directed evolution and rational design. The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. Ala21 is part of an α-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme. © Springer-Verlag 2010 |
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Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents |
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The best mutants (up to 520% wt-activity with MTEA) revealed mutations in the FAD- (A21V, G62D, I69V) and substrate-binding site (S348L, V349L, F351Y). In a separate screening of a library comprising of randomly mutagenised An_CodA, with the natural substrate choline, four mutations were identified, which were further combined in one clone. The constructed clone showed improved activity towards both substrates, MTEA and choline. Mapping these mutation sites onto the structural model of An_CodA revealed that Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate. 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