dc.contributor.author |
Adesioye, Fiyinfoluwa Adenike
|
|
dc.contributor.author |
Makhalanyane, Thulani Peter
|
|
dc.contributor.author |
Vikram, Surendra
|
|
dc.contributor.author |
Sewell, Bryan T.
|
|
dc.contributor.author |
Schubert, Wolf-Dieter
|
|
dc.contributor.author |
Cowan, Don A.
|
|
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 |