Structural characterization and directed evolution of a novel acetyl xylan esterase reveals thermostability determinants of the carbohydrate esterase 7 family
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| dc.contributor.author | Adesioye, Fiyinfoluwa Adenike
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| dc.contributor.author | Makhalanyane, Thulani Peter
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| dc.contributor.author | Vikram, Surendra
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| dc.contributor.author | Sewell, Bryan T.
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| dc.contributor.author | Schubert, Wolf-Dieter
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| dc.contributor.author | Cowan, Don A.
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| dc.date.accessioned | 2018-04-20T10:19:35Z | |
| dc.date.issued | 2018-04 | |
| dc.description.abstract | Please read abstract in the article. | en_ZA |
| dc.description.department | Biochemistry | en_ZA |
| dc.description.department | Genetics | en_ZA |
| dc.description.embargo | 2018-10-01 | |
| dc.description.librarian | hj2018 | en_ZA |
| dc.description.sponsorship | The South Africa Bio-catalysis Initiative, Department of Science and Technology, the University of Pretoria Genomics Research Institute (D.A.C. and T.P.M.), the National Research Foundation (W.-D.S. and B.T.S.), the Research Development Program (T.P.M. and S.V.), and the Organization for Women in Science in the Developing World (OWSD) (F.A.A.). | en_ZA |
| dc.description.uri | http://aem.asm.org | en_ZA |
| dc.identifier.citation | Adesioye FA, Makhalanyane TP, Vikram S, Sewell BT, Schubert W-D, Cowan DA. 2018. Structural characterization and directed evolution of a novel acetyl xylan esterase reveals thermostability determinants of the carbohydrate esterase 7 family. Appl Environ Microbiol 84:e02695-17. https://doi.org/10.1128/AEM.02695-17. | en_ZA |
| dc.identifier.issn | 0099-2240 (print) | |
| dc.identifier.issn | 1098-5336 (online) | |
| dc.identifier.other | 10.1128/AEM.02695-17 | |
| dc.identifier.uri | http://hdl.handle.net/2263/64669 | |
| dc.language.iso | en | en_ZA |
| dc.publisher | American Society for Microbiology | en_ZA |
| dc.rights | © 2018, American Society for Microbiology. All Rights Reserved. | en_ZA |
| dc.subject | X-ray crystallography | en_ZA |
| dc.subject | Structural characterization | en_ZA |
| dc.subject | Single-point mutation | en_ZA |
| dc.subject | Salt concentration | en_ZA |
| dc.subject | Metagenomics | en_ZA |
| dc.subject | Directed evolution | en_ZA |
| dc.subject | Catalytic efficiencies | en_ZA |
| dc.subject | Biosynthesis | en_ZA |
| dc.subject | Carbohydrates | en_ZA |
| dc.subject | Catalyst activity | en_ZA |
| dc.subject | Cloning | en_ZA |
| dc.subject | Crystal structure | en_ZA |
| dc.subject | Efficiency | en_ZA |
| dc.subject | Enzymes | en_ZA |
| dc.subject | Esters | en_ZA |
| dc.subject | Genes | en_ZA |
| dc.subject | Sodium compounds | en_ZA |
| dc.subject | Thermodynamic stability | en_ZA |
| dc.subject | Acetyl xylan esterase (AcXE) | en_ZA |
| dc.subject | Carbohydrate esterase 7 (CE7) | en_ZA |
| dc.subject | Sequence-based metagenomics | en_ZA |
| dc.subject | Thermal stability | en_ZA |
| dc.title | Structural characterization and directed evolution of a novel acetyl xylan esterase reveals thermostability determinants of the carbohydrate esterase 7 family | en_ZA |
| dc.type | Postprint Article | en_ZA |
