Carbohydrate active enzyme domains from extreme thermophiles : components of a modular toolbox for lignocellulose degradation

dc.contributor.authorBotha, Jonathan
dc.contributor.authorMizrachi, Eshchar
dc.contributor.authorMyburg, Alexander Andrew
dc.contributor.authorCowan, Don A.
dc.contributor.emaildon.cowan@up.ac.zaen_ZA
dc.date.accessioned2018-02-07T07:17:49Z
dc.date.issued2018-01
dc.descriptionSupplementary material 1 (XLSX 13 kb)en_ZA
dc.descriptionSupplementary material 2 : Online Resource 2 CAZyme domains identified from extremely thermophilic organisms proteomes using HMMER analysis (PDF 44 kb)en_ZA
dc.descriptionSupplementary material 3 (DOCX 80 kb)en_ZA
dc.description.abstractLignocellulosic 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.en_ZA
dc.description.departmentForestry and Agricultural Biotechnology Institute (FABI)en_ZA
dc.description.departmentGeneticsen_ZA
dc.description.embargo2019-01-30
dc.description.librarianhj2018en_ZA
dc.description.sponsorshipThe National Research Foundation (South Africa)en_ZA
dc.description.urihttp://link.springer.com/journal/792en_ZA
dc.identifier.citationBotha, J., Mizrachi, E., Myburg, A.A. et al. Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation. Extremophiles (2018) 22: 1-12. https://doi.org/10.1007/s00792-017-0974-7.en_ZA
dc.identifier.issn1431-0651 (print)
dc.identifier.issn1433-4909 (online)
dc.identifier.other10.1007/s00792-017-0974-7
dc.identifier.urihttp://hdl.handle.net/2263/63874
dc.language.isoenen_ZA
dc.publisherSpringeren_ZA
dc.rights© Springer Japan KK 2017. The original publication is available at : http://link.springer.comjournal/792.en_ZA
dc.subjectCarbohydrate active enzymes (CAZymes)en_ZA
dc.subjectLignocelluloseen_ZA
dc.subjectExtreme thermophilesen_ZA
dc.subjectSynthetic biologyen_ZA
dc.subjectProtein domainsen_ZA
dc.titleCarbohydrate active enzyme domains from extreme thermophiles : components of a modular toolbox for lignocellulose degradationen_ZA
dc.typePostprint Articleen_ZA

Files

Original bundle

Now showing 1 - 4 of 4
Loading...
Thumbnail Image
Name:
Botha_Carbohydrate_2018.pdf
Size:
556.57 KB
Format:
Adobe Portable Document Format
Description:
Postprint Article
Loading...
Thumbnail Image
Name:
Botha_CarbohydrateSuppl1_2018.xlsx
Size:
14.2 KB
Format:
Microsoft Excel XML
Description:
Supplementary Material 1
Loading...
Thumbnail Image
Name:
Botha_CarbohydrateSuppl2_2018.pdf
Size:
46.86 KB
Format:
Adobe Portable Document Format
Description:
Supplementary Material 2
Loading...
Thumbnail Image
Name:
Botha_CarbohydrateSuppl3_2018.pdf
Size:
186.78 KB
Format:
Adobe Portable Document Format
Description:
Supplementary Material 3

License bundle

Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
license.txt
Size:
1.75 KB
Format:
Item-specific license agreed upon to submission
Description: