dc.contributor.advisor | Le Roes-Hill, Marilize | |
dc.contributor.advisor | McCullough, Bronwyn Kirby | |
dc.contributor.author | Groep, Juandré | |
dc.date.accessioned | 2024-07-29T13:30:44Z | |
dc.date.available | 2024-07-29T13:30:44Z | |
dc.date.issued | 2024 | |
dc.identifier.uri | http://hdl.handle.net/11394/10835 | |
dc.description | >Magister Scientiae - MSc | en_US |
dc.description.abstract | Twenty-one whole genome actinobacterial sequences were obtained from strains previously isolated from various environments. A genome-mining approach was applied to identify the presence of Dye-decolourising (DyP-type or DyPs) peroxidases. From genome sequence annotation twenty-six DyP-type sequences were identified and through bioinformatic analysis for the presence of twin-arginine translocation (Tat) pathway signal peptides, was classified as belonging to class I (formerly class A) bacterial DyP-type peroxidases. Phylogenetic analysis of the DyP sequences showed that the Streptomyces derived DyPs were predominantly grouping together and the nonStreptomyces derived DyPs followed the same pattern. Eight DyP-type peroxidases were selected for cloning, with the majority being derived from Streptomyces spp., and primers were designed to amplify the DyP-type peroxidase genes. The PCR-amplicons were subjected to restriction digests and were ligated into pET20b(+). The constructs were transformed into Escherichia coli JM109. | en_US |
dc.language.iso | en | en_US |
dc.publisher | University of the Western Cape | en_US |
dc.subject | Actinobacteria | en_US |
dc.subject | peroxidase | en_US |
dc.subject | Dye-decoloursing peroxidase | en_US |
dc.subject | DyP-type | en_US |
dc.subject | decolourisation | en_US |
dc.title | Novel DyP-type peroxidases from actinobacteria: a genome mining approach | en_US |
dc.rights.holder | University of the Western Cape | en_US |