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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

Bibliography: pages 127-144.

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Main Author: Louw, Maureen Elizabeth
Other Authors: Reid, Sharon J
Format: Thesis
Language:English
Published: Department of Molecular and Cell Biology 2016
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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