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Bibliography: pages 127-144.
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| Format: | Thesis |
| Language: | English |
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Department of Molecular and Cell Biology
2016
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| _version_ | 1867614012324184064 |
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| access_status_str | Open Access |
| author | Louw, Maureen Elizabeth |
| author2 | Reid, Sharon J |
| author_browse | Louw, Maureen Elizabeth Reid, Sharon J |
| author_facet | Reid, Sharon J Louw, Maureen Elizabeth |
| author_sort | Louw, Maureen Elizabeth |
| collection | Thesis |
| description | Bibliography: pages 127-144. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/21696 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:45:16.514Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2016 |
| publishDateRange | 2016 |
| publishDateSort | 2016 |
| publisher | Department of Molecular and Cell Biology |
| publisherStr | Department of Molecular and Cell Biology |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/21696 Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon Louw, Maureen Elizabeth Reid, Sharon J Molecular and Cell Biology Bibliography: pages 127-144. Bacillus brevis Alk 36 was isolated from soil during a screening programme for the selection of extracellular enzyme producing strains. A gene coding for an endo(1,3- 1,4 )-.8-glucanase (or lichenase) was cloned from B. brevis Alk 36 and expressed in Escherichia coli. The nucleotide sequence of this gene was determined and found to encode a protein of 252 amino acid residues. The amino acid sequence of the B. brevis lichenase gene showed only a 50% similarity to previously published data for Bacillus endo-(1,3-1,4)-β-glucanases. The enzyme exhibited some unique properties. The optimum temperature and pH for enzyme activity were 65-70°C and 8-10, respectively. When held at 75°C for 1 h, 75% residual activity was measured. The molecular mass was estimated to be 29 kDa and the enzyme was found to be resistant to sodium dodecyl sulphate (SDS). B. brevis Alk 36 was evaluated as a potential host strain for the efficient production and secretion of foreign proteins and was found to grow optimally between pH 8.0 and pH 9.5 and between 42°C and 52°C. B. brevis was successfully transformed using vector DNA and was found to produce relatively low levels of protease. In addition, it was evaluated as a possible protein hyper-secreting strain. However, using PCR technology, the highly conserved cell wall protein genes could not be positively identified in B. brevis Alk 36. 2016-09-06T14:44:30Z 2016-09-06T14:44:30Z 1994 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/21696 eng application/pdf Department of Molecular and Cell Biology Faculty of Science University of Cape Town |
| spellingShingle | Molecular and Cell Biology Louw, Maureen Elizabeth Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| thesis_degree_str | Doctoral |
| title | Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| title_full | Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| title_fullStr | Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| title_full_unstemmed | Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| title_short | Characterization of an alkalophilic Bacillus brevis isolate with respect to its endo-(1,3-1,4)-β-glucanase gene, protein hyperproduction and the degS-degU operon |
| title_sort | characterization of an alkalophilic bacillus brevis isolate with respect to its endo 1 3 1 4 β glucanase gene protein hyperproduction and the degs degu operon |
| topic | Molecular and Cell Biology |
| url | http://hdl.handle.net/11427/21696 |
| work_keys_str_mv | AT louwmaureenelizabeth characterizationofanalkalophilicbacillusbrevisisolatewithrespecttoitsendo1314bglucanasegeneproteinhyperproductionandthedegsdeguoperon |