Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application
Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Jäger, Vera D. [verfasserIn] Lamm, Robin [verfasserIn] Küsters, Kira [verfasserIn] Ölçücü, Gizem [verfasserIn] Oldiges, Marco [verfasserIn] Jaeger, Karl-Erich [verfasserIn] Büchs, Jochen [verfasserIn] Krauss, Ulrich [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 104(2020), 17 vom: 10. Juli, Seite 7313-7329 |
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| Übergeordnetes Werk: |
volume:104 ; year:2020 ; number:17 ; day:10 ; month:07 ; pages:7313-7329 |
| Links: |
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| DOI / URN: |
10.1007/s00253-020-10760-3 |
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| Katalog-ID: |
SPR040579654 |
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| 520 | |a Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. | ||
| 650 | 4 | |a Catalytically active inclusion bodies |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Enzyme immobilization |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein engineering |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Synthetic biology |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein co-localization |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Biocatalysis |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Synthetic reaction cascades |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Upstream and downstream processing |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Lamm, Robin |e verfasserin |4 aut | |
| 700 | 1 | |a Küsters, Kira |e verfasserin |4 aut | |
| 700 | 1 | |a Ölçücü, Gizem |e verfasserin |4 aut | |
| 700 | 1 | |a Oldiges, Marco |e verfasserin |4 aut | |
| 700 | 1 | |a Jaeger, Karl-Erich |e verfasserin |4 aut | |
| 700 | 1 | |a Büchs, Jochen |e verfasserin |4 aut | |
| 700 | 1 | |a Krauss, Ulrich |e verfasserin |4 aut | |
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| 773 | 1 | 8 | |g volume:104 |g year:2020 |g number:17 |g day:10 |g month:07 |g pages:7313-7329 |
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10.1007/s00253-020-10760-3 doi (DE-627)SPR040579654 (SPR)s00253-020-10760-3-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Jäger, Vera D. verfasserin aut Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 Lamm, Robin verfasserin aut Küsters, Kira verfasserin aut Ölçücü, Gizem verfasserin aut Oldiges, Marco verfasserin aut Jaeger, Karl-Erich verfasserin aut Büchs, Jochen verfasserin aut Krauss, Ulrich verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 17 vom: 10. Juli, Seite 7313-7329 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 https://dx.doi.org/10.1007/s00253-020-10760-3 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 17 10 07 7313-7329 |
| spelling |
10.1007/s00253-020-10760-3 doi (DE-627)SPR040579654 (SPR)s00253-020-10760-3-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Jäger, Vera D. verfasserin aut Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 Lamm, Robin verfasserin aut Küsters, Kira verfasserin aut Ölçücü, Gizem verfasserin aut Oldiges, Marco verfasserin aut Jaeger, Karl-Erich verfasserin aut Büchs, Jochen verfasserin aut Krauss, Ulrich verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 17 vom: 10. Juli, Seite 7313-7329 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 https://dx.doi.org/10.1007/s00253-020-10760-3 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 17 10 07 7313-7329 |
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10.1007/s00253-020-10760-3 doi (DE-627)SPR040579654 (SPR)s00253-020-10760-3-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Jäger, Vera D. verfasserin aut Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 Lamm, Robin verfasserin aut Küsters, Kira verfasserin aut Ölçücü, Gizem verfasserin aut Oldiges, Marco verfasserin aut Jaeger, Karl-Erich verfasserin aut Büchs, Jochen verfasserin aut Krauss, Ulrich verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 17 vom: 10. Juli, Seite 7313-7329 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 https://dx.doi.org/10.1007/s00253-020-10760-3 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 17 10 07 7313-7329 |
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10.1007/s00253-020-10760-3 doi (DE-627)SPR040579654 (SPR)s00253-020-10760-3-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Jäger, Vera D. verfasserin aut Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 Lamm, Robin verfasserin aut Küsters, Kira verfasserin aut Ölçücü, Gizem verfasserin aut Oldiges, Marco verfasserin aut Jaeger, Karl-Erich verfasserin aut Büchs, Jochen verfasserin aut Krauss, Ulrich verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 17 vom: 10. Juli, Seite 7313-7329 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 https://dx.doi.org/10.1007/s00253-020-10760-3 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 17 10 07 7313-7329 |
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10.1007/s00253-020-10760-3 doi (DE-627)SPR040579654 (SPR)s00253-020-10760-3-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Jäger, Vera D. verfasserin aut Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 Lamm, Robin verfasserin aut Küsters, Kira verfasserin aut Ölçücü, Gizem verfasserin aut Oldiges, Marco verfasserin aut Jaeger, Karl-Erich verfasserin aut Büchs, Jochen verfasserin aut Krauss, Ulrich verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 17 vom: 10. Juli, Seite 7313-7329 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 https://dx.doi.org/10.1007/s00253-020-10760-3 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 17 10 07 7313-7329 |
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Enthalten in Applied microbiology and biotechnology 104(2020), 17 vom: 10. Juli, Seite 7313-7329 volume:104 year:2020 number:17 day:10 month:07 pages:7313-7329 |
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Catalytically active inclusion bodies Enzyme immobilization Protein engineering Synthetic biology Protein co-localization Biocatalysis Synthetic reaction cascades Upstream and downstream processing |
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Applied microbiology and biotechnology |
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Jäger, Vera D. @@aut@@ Lamm, Robin @@aut@@ Küsters, Kira @@aut@@ Ölçücü, Gizem @@aut@@ Oldiges, Marco @@aut@@ Jaeger, Karl-Erich @@aut@@ Büchs, Jochen @@aut@@ Krauss, Ulrich @@aut@@ |
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In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. 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|
| author |
Jäger, Vera D. |
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Jäger, Vera D. ddc 570 bkl 58.30 bkl 42.30 misc Catalytically active inclusion bodies misc Enzyme immobilization misc Protein engineering misc Synthetic biology misc Protein co-localization misc Biocatalysis misc Synthetic reaction cascades misc Upstream and downstream processing Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application |
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Jäger, Vera D. |
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1432-0614 |
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570 ASE 58.30 bkl 42.30 bkl Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application Catalytically active inclusion bodies (dpeaa)DE-He213 Enzyme immobilization (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein co-localization (dpeaa)DE-He213 Biocatalysis (dpeaa)DE-He213 Synthetic reaction cascades (dpeaa)DE-He213 Upstream and downstream processing (dpeaa)DE-He213 |
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ddc 570 bkl 58.30 bkl 42.30 misc Catalytically active inclusion bodies misc Enzyme immobilization misc Protein engineering misc Synthetic biology misc Protein co-localization misc Biocatalysis misc Synthetic reaction cascades misc Upstream and downstream processing |
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ddc 570 bkl 58.30 bkl 42.30 misc Catalytically active inclusion bodies misc Enzyme immobilization misc Protein engineering misc Synthetic biology misc Protein co-localization misc Biocatalysis misc Synthetic reaction cascades misc Upstream and downstream processing |
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ddc 570 bkl 58.30 bkl 42.30 misc Catalytically active inclusion bodies misc Enzyme immobilization misc Protein engineering misc Synthetic biology misc Protein co-localization misc Biocatalysis misc Synthetic reaction cascades misc Upstream and downstream processing |
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Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application |
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Jäger, Vera D. |
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Applied microbiology and biotechnology |
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Jäger, Vera D. Lamm, Robin Küsters, Kira Ölçücü, Gizem Oldiges, Marco Jaeger, Karl-Erich Büchs, Jochen Krauss, Ulrich |
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catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application |
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Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application |
| abstract |
Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. |
| abstractGer |
Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. |
| abstract_unstemmed |
Abstract Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste material produced by heterologous overexpression of recombinant genes. In industrial applications, they are occasionally used as an alternative in cases where a protein cannot be expressed in soluble form and in high enough amounts. Then, however, refolding approaches are needed to transform inactive IBs into active soluble protein. While anecdotal reports about IBs themselves showing catalytic functionality/activity (CatIB) are found throughout literature, only recently, the use of protein engineering methods has facilitated the on-demand production of CatIBs. CatIB formation is induced usually by fusing short peptide tags or aggregation-inducing protein domains to a target protein. The resulting proteinaceous particles formed by heterologous expression of the respective genes can be regarded as a biologically produced bionanomaterial or, if enzymes are used as target protein, carrier-free enzyme immobilizates. In the present contribution, we review general concepts important for CatIB production, processing, and application. Key points • Catalytically active inclusion bodies (CatIBs) are promising bionanomaterials. • Potential applications in biocatalysis, synthetic chemistry, and biotechnology. • CatIB formation represents a generic approach for enzyme immobilization. • CatIB formation efficiency depends on construct design and expression conditions. |
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|
| score |
7.401516 |