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Analysis of dextrin dextranase from Gluconobacter oxydans

Thesis (MSc (Genetics. Institute for Plant Biotechnology (IPB)))--Stellenbosch University, 2008.

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Main Author: Van Wyk, Nathan
Other Authors: Lloyd, James Richard
Format: Thesis
Language:English
Published: Stellenbosch : Stellenbosch University 2008
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access_status_str Open Access
author Van Wyk, Nathan
author2 Lloyd, James Richard
author_browse Lloyd, James Richard
Van Wyk, Nathan
author_facet Lloyd, James Richard
Van Wyk, Nathan
author_sort Van Wyk, Nathan
collection Thesis
dc_rights_str_mv Stellenbosch University
description Thesis (MSc (Genetics. Institute for Plant Biotechnology (IPB)))--Stellenbosch University, 2008.
format Thesis
id oai:scholar.sun.ac.za:10019.1/2619
institution Stellenbosch University (South Africa)
language English
last_indexed 2026-06-10T12:43:16.997Z
license_str Other — see source repository
provenance_str_mv Harvested via OAI-PMH from SUNScholar — Stellenbosch University Repository
publishDate 2008
publishDateRange 2008
publishDateSort 2008
publisher Stellenbosch : Stellenbosch University
publisherStr Stellenbosch : Stellenbosch University
record_format dspace
source_str SUNScholar — Stellenbosch University Repository
spelling oai:scholar.sun.ac.za:10019.1/2619 Analysis of dextrin dextranase from Gluconobacter oxydans Van Wyk, Nathan Lloyd, James Richard Kossmann, J. M. Stellenbosch University. Faculty of AgriSciences. Dept. of Genetics. Institute for Plant Biotechnology. Dextrin dextranase Gluconobacter oxydans Theses -- Plant biotechnology Dissertations -- Plant biotechnology Thesis (MSc (Genetics. Institute for Plant Biotechnology (IPB)))--Stellenbosch University, 2008. Dextran is a high value glucose polymer used in medicine and an array of laboratory techniques. It is synthesised by lactic-acid bacteria from sucrose but has also reportedly been produced by Gluconobacter oxydans (G. oxydans) from a range of maltooligosaccharides (MOS) via the action of dextrin dextranase (DDase). In this study the presence of DDase is investigated in two G. oxydans strains (ATCC 621H and ATCC 19357) and shown to be present in the ATCC 19357 strain, but not in the ATCC 621H strain. The enzyme was partially purified from the ATCC 19357 strain, and its kinetic properties investigated. The partially purified protein was also digested with trypsin, and de novo peptide sequences obtained from it. Several attempts were made to obtain the gene coding for the DDase. These include amplifying an open reading frame from the G. oxydans genome coding for a glycosyltransferase with the approximate molecular weight of the DDase, using the peptide sequences obtained from the partially purified protein to design degenerate PCR primers and the production of a genomic DNA library for functional screening in E. coli. None of these approaches led to the successful isolation of the extracellular DDase sequence. Masters 2008-11-21T06:50:50Z 2010-06-01T08:53:46Z 2008-11-21T06:50:50Z 2010-06-01T08:53:46Z 2008-12 Thesis http://hdl.handle.net/10019.1/2619 en Stellenbosch University application/pdf Stellenbosch : Stellenbosch University
spellingShingle Dextrin dextranase
Gluconobacter oxydans
Theses -- Plant biotechnology
Dissertations -- Plant biotechnology
Van Wyk, Nathan
Analysis of dextrin dextranase from Gluconobacter oxydans
title Analysis of dextrin dextranase from Gluconobacter oxydans
title_full Analysis of dextrin dextranase from Gluconobacter oxydans
title_fullStr Analysis of dextrin dextranase from Gluconobacter oxydans
title_full_unstemmed Analysis of dextrin dextranase from Gluconobacter oxydans
title_short Analysis of dextrin dextranase from Gluconobacter oxydans
title_sort analysis of dextrin dextranase from gluconobacter oxydans
topic Dextrin dextranase
Gluconobacter oxydans
Theses -- Plant biotechnology
Dissertations -- Plant biotechnology
url http://hdl.handle.net/10019.1/2619
work_keys_str_mv AT vanwyknathan analysisofdextrindextranasefromgluconobacteroxydans