Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation
Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymeri...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Botha, Jonathan [verfasserIn] Mizrachi, Eshchar [verfasserIn] Myburg, Alexander A. [verfasserIn] Cowan, Don A. [verfasserIn] |
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E-Artikel |
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Englisch |
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2017 |
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Enthalten in: Extremophiles - Springer-Verlag, 2001, 22(2017), 1 vom: 06. Nov., Seite 1-12 |
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volume:22 ; year:2017 ; number:1 ; day:06 ; month:11 ; pages:1-12 |
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10.1007/s00792-017-0974-7 |
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| 520 | |a Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. | ||
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10.1007/s00792-017-0974-7 doi (DE-627)SPR007866283 (SPR)s00792-017-0974-7-e DE-627 ger DE-627 rakwb eng Botha, Jonathan verfasserin aut Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. Lignocellulose (dpeaa)DE-He213 CAZyme (dpeaa)DE-He213 Extreme thermophiles (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein domains (dpeaa)DE-He213 Mizrachi, Eshchar verfasserin aut Myburg, Alexander A. verfasserin aut Cowan, Don A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 22(2017), 1 vom: 06. Nov., Seite 1-12 (DE-627)SPR007852657 nnns volume:22 year:2017 number:1 day:06 month:11 pages:1-12 https://dx.doi.org/10.1007/s00792-017-0974-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 22 2017 1 06 11 1-12 |
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10.1007/s00792-017-0974-7 doi (DE-627)SPR007866283 (SPR)s00792-017-0974-7-e DE-627 ger DE-627 rakwb eng Botha, Jonathan verfasserin aut Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. Lignocellulose (dpeaa)DE-He213 CAZyme (dpeaa)DE-He213 Extreme thermophiles (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein domains (dpeaa)DE-He213 Mizrachi, Eshchar verfasserin aut Myburg, Alexander A. verfasserin aut Cowan, Don A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 22(2017), 1 vom: 06. Nov., Seite 1-12 (DE-627)SPR007852657 nnns volume:22 year:2017 number:1 day:06 month:11 pages:1-12 https://dx.doi.org/10.1007/s00792-017-0974-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 22 2017 1 06 11 1-12 |
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10.1007/s00792-017-0974-7 doi (DE-627)SPR007866283 (SPR)s00792-017-0974-7-e DE-627 ger DE-627 rakwb eng Botha, Jonathan verfasserin aut Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. Lignocellulose (dpeaa)DE-He213 CAZyme (dpeaa)DE-He213 Extreme thermophiles (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein domains (dpeaa)DE-He213 Mizrachi, Eshchar verfasserin aut Myburg, Alexander A. verfasserin aut Cowan, Don A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 22(2017), 1 vom: 06. Nov., Seite 1-12 (DE-627)SPR007852657 nnns volume:22 year:2017 number:1 day:06 month:11 pages:1-12 https://dx.doi.org/10.1007/s00792-017-0974-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 22 2017 1 06 11 1-12 |
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10.1007/s00792-017-0974-7 doi (DE-627)SPR007866283 (SPR)s00792-017-0974-7-e DE-627 ger DE-627 rakwb eng Botha, Jonathan verfasserin aut Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. Lignocellulose (dpeaa)DE-He213 CAZyme (dpeaa)DE-He213 Extreme thermophiles (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein domains (dpeaa)DE-He213 Mizrachi, Eshchar verfasserin aut Myburg, Alexander A. verfasserin aut Cowan, Don A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 22(2017), 1 vom: 06. Nov., Seite 1-12 (DE-627)SPR007852657 nnns volume:22 year:2017 number:1 day:06 month:11 pages:1-12 https://dx.doi.org/10.1007/s00792-017-0974-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 22 2017 1 06 11 1-12 |
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10.1007/s00792-017-0974-7 doi (DE-627)SPR007866283 (SPR)s00792-017-0974-7-e DE-627 ger DE-627 rakwb eng Botha, Jonathan verfasserin aut Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. Lignocellulose (dpeaa)DE-He213 CAZyme (dpeaa)DE-He213 Extreme thermophiles (dpeaa)DE-He213 Synthetic biology (dpeaa)DE-He213 Protein domains (dpeaa)DE-He213 Mizrachi, Eshchar verfasserin aut Myburg, Alexander A. verfasserin aut Cowan, Don A. verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 22(2017), 1 vom: 06. Nov., Seite 1-12 (DE-627)SPR007852657 nnns volume:22 year:2017 number:1 day:06 month:11 pages:1-12 https://dx.doi.org/10.1007/s00792-017-0974-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 22 2017 1 06 11 1-12 |
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Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation |
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Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. |
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Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. |
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Abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. |
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Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation |
| url |
https://dx.doi.org/10.1007/s00792-017-0974-7 |
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true |
| author2 |
Mizrachi, Eshchar Myburg, Alexander A. Cowan, Don A. |
| author2Str |
Mizrachi, Eshchar Myburg, Alexander A. Cowan, Don A. |
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SPR007852657 |
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c |
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| doi_str |
10.1007/s00792-017-0974-7 |
| up_date |
2024-07-03T15:45:01.343Z |
| _version_ |
1803573265789091840 |
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However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. 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7.399705 |