E Pass Office
- Ndlovu, Jackson, not specified, T. Buson, Tracey, Hugh
- Authors: Ndlovu, Jackson , not specified , T. Buson , Tracey, Hugh
- Date: 0000-00-00
- Subjects: Popular music--Africa , Field recordings , Africa, Sub-Saharan , Africa South Africa city not specified f-sa
- Language: Zulu
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/235695 , vital:50332 , International Library of African Music, Rhodes University, Makhanda, South Africa , Hugh Tracey Commercial Records, Rhodes University, Makhanda, South Africa , CR2880 , ABC16374
- Description: A Zulu Sketch
- Full Text: false
- Date Issued: 0000-00-00
- Authors: Ndlovu, Jackson , not specified , T. Buson , Tracey, Hugh
- Date: 0000-00-00
- Subjects: Popular music--Africa , Field recordings , Africa, Sub-Saharan , Africa South Africa city not specified f-sa
- Language: Zulu
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/235695 , vital:50332 , International Library of African Music, Rhodes University, Makhanda, South Africa , Hugh Tracey Commercial Records, Rhodes University, Makhanda, South Africa , CR2880 , ABC16374
- Description: A Zulu Sketch
- Full Text: false
- Date Issued: 0000-00-00
Inyanga
- Ndlovu, Jackson, not specified, T. Buson, Tracey, Hugh
- Authors: Ndlovu, Jackson , not specified , T. Buson , Tracey, Hugh
- Date: 0000-00-00
- Subjects: Popular music--Africa , Field recordings , Africa, Sub-Saharan , Africa South Africa city not specified f-sa
- Language: Zulu
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/235704 , vital:50333 , International Library of African Music, Rhodes University, Makhanda, South Africa , Hugh Tracey Commercial Records, Rhodes University, Makhanda, South Africa , CR2880 , ABC16375
- Description: A Zulu Sketch
- Full Text: false
- Date Issued: 0000-00-00
- Authors: Ndlovu, Jackson , not specified , T. Buson , Tracey, Hugh
- Date: 0000-00-00
- Subjects: Popular music--Africa , Field recordings , Africa, Sub-Saharan , Africa South Africa city not specified f-sa
- Language: Zulu
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/235704 , vital:50333 , International Library of African Music, Rhodes University, Makhanda, South Africa , Hugh Tracey Commercial Records, Rhodes University, Makhanda, South Africa , CR2880 , ABC16375
- Description: A Zulu Sketch
- Full Text: false
- Date Issued: 0000-00-00
Development of a hydantoin-hydrolysing biocatalyst for the production of optically pure amino acids using Agrobacterium tumefaciens strain RU-ORPN1
- Authors: Foster, Ingrid Margaret
- Date: 2004
- Subjects: Agrobacterium tumefaciens Amino acids Hydantoin Hydrolysis Enzymes
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3943 , http://hdl.handle.net/10962/d1004002
- Description: A calcium alginate bead-immobilised biocatalyst was developed utilising the D-hydantoinase and D-N-carbamoylase from a novel, mutant Agrobacterium tumefaciens strain RU-ORPN1. The growth conditions for the inducer-independent strain were optimised for production of hydantoinase and N-carbamoylase activities. Methods for the preparation of crude enzyme extracts were evaluated in terms of hydantoinase and N-carbamoylase activities produced. After comparison of the enzyme activities and stabilities in various extracts from fresh and frozen cells, sonication of frozen cells for 5 minutes was found to be the best method for the production of the enzyme extract. The optimal pH and temperature for the hydantoinase activity were pH 10 and 30°C, respectively, while pH 9 and 40°C were optimal for Ncarbamoylase activity. The hydantoinase activity was enhanced by the addition of Mg^(2+) ions to the enzyme extract and the N-carbamoylase was enhanced by the addition of Mg^(2+), Mn^(2+) or Zn^(2+) ions to the enzyme extract. The enzyme activities increased in the presence of ATP suggesting that the enzymes may be ATP-dependent. The addition of DTT and PMSF to the enzyme extract enhanced the hydantoinase activity but had no effect on the N-carbamoylase activity. The N-carbamoylase was unstable at 40°C and was almost completely inactivated after 24 hours incubation at this temperature. The hydantoinase and N-carbamoylase appeared to be insoluble. Various techniques were investigated for the solubilisation of the enzymes including various cell lysis methods, cell lysis at extremes of pH and ionic strength, addition of a reducing agent and protease inhibitors, and treatment with hydrolysing enzymes and detergents. Treatment with Triton X-100 was most effective for the solubilisation of the enzymes indicating that the enzymes were membrane-bound. Hydropathy and transmembrane prediction plots of the predicted amino acid sequences for two identified N-carbamoylase genes from A. tumefaciens RU-ORPN1 revealed possible transmembrane regions in the amino acid sequences, and thus supported the hypothesis that the enzymes were membrane-bound. Various methods were evaluated for the immobilisation of the enzymes in whole cells and enzyme extracts. Immobilisation of the enzyme extract in calcium alginate beads was found to be the best method in terms of enzyme activity retention and stability. The hydantoinase retained 55% activity while the N-carbamoylase exhibited a remarkable sevenfold increase in activity after immobilisation by this method. Furthermore, the hydantoinase activity increased after storage at 4°C for 21 days, while the N-carbamoylase retained 30% activity after this storage period. The calcium alginate bead-immobilised enzymes were further biochemically characterised and then applied in a bioreactor system for the production of D-hydroxyphenylglycine (D-HPG) from D,L-5-hydroxyphenylhydantoin (D,L-5-HPH). The pH and temperature optima for the immobilised hydantoinase were pH 7 and 50°C, respectively, while pH 8 and 40°C were optimal for the immobilised N-carbamoylase enzyme. The immobilised enzymes showed improved thermostability at 40°C in comparison to the free enzymes and retained high levels of activity after five repeated batch reactions. Low levels of conversion were obtained in a packed-bed bioreactor containing the A. tumefaciens RU-ORPN1 biocatalyst due to the low hydantoinase activity present in the strain, relative to N-carbamoylase. A novel, packed-bed bioreactor system was therefore developed for the production of D-HPG from D,L-5-HPH using the A. tumefaciens biocatalyst in combination with a Pseudomonas sp. biocatalyst having high hydantoinase activity. A conversion yield of 22 to 30% was achieved for the production of D-HPG from D,L-5-HPH over 5 days operation demonstrating that the hydantoin-hydrolysing enzymes from A. tumefaciens RU-ORPN1 could be stabilised by immobilisation and, in combination with a biocatalyst with high hydantoinase activity, could be applied to the fully enzymatic conversion of D,L-5-HPH to D-HPG.
- Full Text:
- Date Issued: 2004
- Authors: Foster, Ingrid Margaret
- Date: 2004
- Subjects: Agrobacterium tumefaciens Amino acids Hydantoin Hydrolysis Enzymes
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3943 , http://hdl.handle.net/10962/d1004002
- Description: A calcium alginate bead-immobilised biocatalyst was developed utilising the D-hydantoinase and D-N-carbamoylase from a novel, mutant Agrobacterium tumefaciens strain RU-ORPN1. The growth conditions for the inducer-independent strain were optimised for production of hydantoinase and N-carbamoylase activities. Methods for the preparation of crude enzyme extracts were evaluated in terms of hydantoinase and N-carbamoylase activities produced. After comparison of the enzyme activities and stabilities in various extracts from fresh and frozen cells, sonication of frozen cells for 5 minutes was found to be the best method for the production of the enzyme extract. The optimal pH and temperature for the hydantoinase activity were pH 10 and 30°C, respectively, while pH 9 and 40°C were optimal for Ncarbamoylase activity. The hydantoinase activity was enhanced by the addition of Mg^(2+) ions to the enzyme extract and the N-carbamoylase was enhanced by the addition of Mg^(2+), Mn^(2+) or Zn^(2+) ions to the enzyme extract. The enzyme activities increased in the presence of ATP suggesting that the enzymes may be ATP-dependent. The addition of DTT and PMSF to the enzyme extract enhanced the hydantoinase activity but had no effect on the N-carbamoylase activity. The N-carbamoylase was unstable at 40°C and was almost completely inactivated after 24 hours incubation at this temperature. The hydantoinase and N-carbamoylase appeared to be insoluble. Various techniques were investigated for the solubilisation of the enzymes including various cell lysis methods, cell lysis at extremes of pH and ionic strength, addition of a reducing agent and protease inhibitors, and treatment with hydrolysing enzymes and detergents. Treatment with Triton X-100 was most effective for the solubilisation of the enzymes indicating that the enzymes were membrane-bound. Hydropathy and transmembrane prediction plots of the predicted amino acid sequences for two identified N-carbamoylase genes from A. tumefaciens RU-ORPN1 revealed possible transmembrane regions in the amino acid sequences, and thus supported the hypothesis that the enzymes were membrane-bound. Various methods were evaluated for the immobilisation of the enzymes in whole cells and enzyme extracts. Immobilisation of the enzyme extract in calcium alginate beads was found to be the best method in terms of enzyme activity retention and stability. The hydantoinase retained 55% activity while the N-carbamoylase exhibited a remarkable sevenfold increase in activity after immobilisation by this method. Furthermore, the hydantoinase activity increased after storage at 4°C for 21 days, while the N-carbamoylase retained 30% activity after this storage period. The calcium alginate bead-immobilised enzymes were further biochemically characterised and then applied in a bioreactor system for the production of D-hydroxyphenylglycine (D-HPG) from D,L-5-hydroxyphenylhydantoin (D,L-5-HPH). The pH and temperature optima for the immobilised hydantoinase were pH 7 and 50°C, respectively, while pH 8 and 40°C were optimal for the immobilised N-carbamoylase enzyme. The immobilised enzymes showed improved thermostability at 40°C in comparison to the free enzymes and retained high levels of activity after five repeated batch reactions. Low levels of conversion were obtained in a packed-bed bioreactor containing the A. tumefaciens RU-ORPN1 biocatalyst due to the low hydantoinase activity present in the strain, relative to N-carbamoylase. A novel, packed-bed bioreactor system was therefore developed for the production of D-HPG from D,L-5-HPH using the A. tumefaciens biocatalyst in combination with a Pseudomonas sp. biocatalyst having high hydantoinase activity. A conversion yield of 22 to 30% was achieved for the production of D-HPG from D,L-5-HPH over 5 days operation demonstrating that the hydantoin-hydrolysing enzymes from A. tumefaciens RU-ORPN1 could be stabilised by immobilisation and, in combination with a biocatalyst with high hydantoinase activity, could be applied to the fully enzymatic conversion of D,L-5-HPH to D-HPG.
- Full Text:
- Date Issued: 2004
Elucidation and manipulation of the Hydantoin-Hydrolysing Enzyme System of Agrobacterium tumefaciens RU-OR for the Biocatalytic production of D-amino acids
- Authors: Hartley, Carol Janet
- Date: 2002
- Subjects: Amino acids Agrobacterium tumefaciens
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3916 , http://hdl.handle.net/10962/d1003975
- Description: There is widespread interest in the biocatalytic production of enantiomerically pure D-amino acids for use in the synthesis of antibiotics, insecticides, herbicides, drug carriers and many other pharmaceuticals. Hydantoin-hydrolysing enzyme systems can be successfully utilised to stereoselectively convert racemic hydantoins into enantiomerically pure amino acid products. In fact, the use of microbial D-hydantoinase and D-stereoselective N-carbamoyl amino acid amidohydrolase activity to produce D-p-hydroxyphenylglycine from D,L-5-phydroxyphenylhydantoin has been described as one of the most successful biotechnological applications of enzyme technology developed to date. A need to utilise the novel biodiversity of South African microorganisms for the development of an indigenous process to produce enantiomerically pure amino acids was identified in 1995. Subsequently, the Rhodes Hydantoinase Group was established and several local hydantoin-hydrolysing microorganisms were isolated. The research in this study describes the isolation and selection of Agrobacterium tumefaciens RU-OR, which produced D-stereoselective hydantoinhydrolysing activity. Characterisation of the hydantoin-hydrolysing enzyme system of RU-OR revealed novel biocatalytic properties, and potential for the application of this strain for the biocatalytic production of D-amino acids. A fundamental understanding of the regulation of hydantoin-hydrolysing enzyme activity in A. tumefaciens RU-OR was established, and utilised to produce mutant strains with altered regulation of hydantoin-hydrolysing activity. These strains were used to further elucidate the mechanisms regulating the production of hydantoins-hydrolysing activity in A. tumefaciens RU-OR cells. Overproduction of hydantoinase and N-carbamoyl-D-amino acid amidohydrolase activity in selected mutant strains resulted in efficient conversion of D,L-5-p-hydroxyphenylhydantoin to D-p-hydroxyphenylglycine. Thus the establishment of a primary understanding of the hydantoin-hydrolysing enzyme system in A. tumefaciens RU-OR could be used to manipulate the hydantoin-hydrolysing activity in RU-OR cells to produce an improved biocatalyst. The isolation of A. tumfecaiens RU-OR genes encoding for hydantoin-hydrolysing activity revealed two separate N-carbamoyl-D-amino acid amidohydrolaseencoding genes (ncaR1 and ncaR2) in this bacterium with distinct chromosomal locations, nucleotide coding sequence and predicted primary amino acid sequence. The novel biocatalytic properties of the hydantoin-hydrolysing enzyme system in A. tumefaciens RU-OR and mutant derivatives present fascinating opportunities for further elucidation of the natural function, regulation and biocatalytic potential of hydantoin-hydrolysing enzymes.
- Full Text:
- Date Issued: 2002
- Authors: Hartley, Carol Janet
- Date: 2002
- Subjects: Amino acids Agrobacterium tumefaciens
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3916 , http://hdl.handle.net/10962/d1003975
- Description: There is widespread interest in the biocatalytic production of enantiomerically pure D-amino acids for use in the synthesis of antibiotics, insecticides, herbicides, drug carriers and many other pharmaceuticals. Hydantoin-hydrolysing enzyme systems can be successfully utilised to stereoselectively convert racemic hydantoins into enantiomerically pure amino acid products. In fact, the use of microbial D-hydantoinase and D-stereoselective N-carbamoyl amino acid amidohydrolase activity to produce D-p-hydroxyphenylglycine from D,L-5-phydroxyphenylhydantoin has been described as one of the most successful biotechnological applications of enzyme technology developed to date. A need to utilise the novel biodiversity of South African microorganisms for the development of an indigenous process to produce enantiomerically pure amino acids was identified in 1995. Subsequently, the Rhodes Hydantoinase Group was established and several local hydantoin-hydrolysing microorganisms were isolated. The research in this study describes the isolation and selection of Agrobacterium tumefaciens RU-OR, which produced D-stereoselective hydantoinhydrolysing activity. Characterisation of the hydantoin-hydrolysing enzyme system of RU-OR revealed novel biocatalytic properties, and potential for the application of this strain for the biocatalytic production of D-amino acids. A fundamental understanding of the regulation of hydantoin-hydrolysing enzyme activity in A. tumefaciens RU-OR was established, and utilised to produce mutant strains with altered regulation of hydantoin-hydrolysing activity. These strains were used to further elucidate the mechanisms regulating the production of hydantoins-hydrolysing activity in A. tumefaciens RU-OR cells. Overproduction of hydantoinase and N-carbamoyl-D-amino acid amidohydrolase activity in selected mutant strains resulted in efficient conversion of D,L-5-p-hydroxyphenylhydantoin to D-p-hydroxyphenylglycine. Thus the establishment of a primary understanding of the hydantoin-hydrolysing enzyme system in A. tumefaciens RU-OR could be used to manipulate the hydantoin-hydrolysing activity in RU-OR cells to produce an improved biocatalyst. The isolation of A. tumfecaiens RU-OR genes encoding for hydantoin-hydrolysing activity revealed two separate N-carbamoyl-D-amino acid amidohydrolaseencoding genes (ncaR1 and ncaR2) in this bacterium with distinct chromosomal locations, nucleotide coding sequence and predicted primary amino acid sequence. The novel biocatalytic properties of the hydantoin-hydrolysing enzyme system in A. tumefaciens RU-OR and mutant derivatives present fascinating opportunities for further elucidation of the natural function, regulation and biocatalytic potential of hydantoin-hydrolysing enzymes.
- Full Text:
- Date Issued: 2002
Characterization of the hydantoin-hydrolysing system of Pseudomonas putida RU-KM3s
- Authors: Matcher, Gwynneth Felicity
- Date: 2005
- Subjects: Hydantoin Hydrolysis Pseudomonas Enzymes
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3939 , http://hdl.handle.net/10962/d1003998
- Description: The biocatalytic conversion of 5-monosubstituted hydantoin derivatives to optically pure amino acids involves two reaction steps: the hydrolysis of hydantoin to N-carbamylamino acid by an hydantoinase or dihydropyrimidinase enzyme, followed by conversion of the Ncarbamylamino acid to the corresponding amino acid by an N-carbamoylase enzyme. This biocatalytic process has been successfully applied in several industrial processes for the production of enantiomerically pure amino acids used in the synthesis of pharmaceuticals, insecticides, hormones, and food additives. P. putida RU-KM3S was selected for study based on inherent high levels of hydantoinase and N-carbamoylase activity. Subsequent biocatalytic analysis of the enzyme activity within this strain revealed unique properties thus prompting further characterization. The main focus of this research was the isolation of the genes encoding the hydantoin-hydrolysing pathway in RU-KM3S. A genomic library was constructed and screened for heterologous expression of the hydantoin-hydrolysing enzymes. However, this approach was unsuccessful prompting the use of transposon mutagenesis in order to circumvent the drawbacks associated with complementation studies. The enzymes responsible for hydantoin-hydrolysis were identified by insertional inactivation as a dihydropyrimidinase and b-ureidopropionase encoded by dhp and bup respectively. A third open reading frame, encoding a putative transport protein, was identified between the dhp and bup genes and appeared to share a promoter with bup. Analysis of the amino acid sequence deduced from bup and dhp substantiated the distinctive properties and potential industrial application of the L-enantioselective b-ureidopropionase and provided targets for potential optimisation of the substrate-selectivity and activity of the dihydropyrimidinase by site directed mutagenesis. Several transposon-generated mutants with an altered phenotype for growth on minimal medium with hydantoin as the sole source of nitrogen were also isolated. Analysis of the insertion events in these mutants revealed disruptions of genes encoding key elements of the Ntr global regulatory pathway. However, inactivation of these genes had no effect on the dihydropyrimidinase and b-ureidopropionase activity levels. An additional mutant in which the gene coding for the dihydrolipoamide succinyltransferase, which is involved in the TCA cycle, was isolated with reduced levels of both dihydropyrimidinase and b-ureidopropionase activities. These results indicated that the hydantoin-hydrolysis pathway in RU-KM3S is regulated by carbon rather than nitrogen catabolite repression. This was confirmed by the reduction of hydantoin-hydrolysis in cells grown in excess carbon as opposed to nitrogen. Identification of a putative CRP-binding site within the promoter region of these enzymes further supported the regulatory role of carbon catabolite repression (CCR). As CCR in Pseudomonads is poorly understood, elucidation of the mechanism by which the hydantoinhydrolysing pathway in RU-KM3S is regulated would provide valuable insight into this complex process.
- Full Text:
- Date Issued: 2005
- Authors: Matcher, Gwynneth Felicity
- Date: 2005
- Subjects: Hydantoin Hydrolysis Pseudomonas Enzymes
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3939 , http://hdl.handle.net/10962/d1003998
- Description: The biocatalytic conversion of 5-monosubstituted hydantoin derivatives to optically pure amino acids involves two reaction steps: the hydrolysis of hydantoin to N-carbamylamino acid by an hydantoinase or dihydropyrimidinase enzyme, followed by conversion of the Ncarbamylamino acid to the corresponding amino acid by an N-carbamoylase enzyme. This biocatalytic process has been successfully applied in several industrial processes for the production of enantiomerically pure amino acids used in the synthesis of pharmaceuticals, insecticides, hormones, and food additives. P. putida RU-KM3S was selected for study based on inherent high levels of hydantoinase and N-carbamoylase activity. Subsequent biocatalytic analysis of the enzyme activity within this strain revealed unique properties thus prompting further characterization. The main focus of this research was the isolation of the genes encoding the hydantoin-hydrolysing pathway in RU-KM3S. A genomic library was constructed and screened for heterologous expression of the hydantoin-hydrolysing enzymes. However, this approach was unsuccessful prompting the use of transposon mutagenesis in order to circumvent the drawbacks associated with complementation studies. The enzymes responsible for hydantoin-hydrolysis were identified by insertional inactivation as a dihydropyrimidinase and b-ureidopropionase encoded by dhp and bup respectively. A third open reading frame, encoding a putative transport protein, was identified between the dhp and bup genes and appeared to share a promoter with bup. Analysis of the amino acid sequence deduced from bup and dhp substantiated the distinctive properties and potential industrial application of the L-enantioselective b-ureidopropionase and provided targets for potential optimisation of the substrate-selectivity and activity of the dihydropyrimidinase by site directed mutagenesis. Several transposon-generated mutants with an altered phenotype for growth on minimal medium with hydantoin as the sole source of nitrogen were also isolated. Analysis of the insertion events in these mutants revealed disruptions of genes encoding key elements of the Ntr global regulatory pathway. However, inactivation of these genes had no effect on the dihydropyrimidinase and b-ureidopropionase activity levels. An additional mutant in which the gene coding for the dihydrolipoamide succinyltransferase, which is involved in the TCA cycle, was isolated with reduced levels of both dihydropyrimidinase and b-ureidopropionase activities. These results indicated that the hydantoin-hydrolysis pathway in RU-KM3S is regulated by carbon rather than nitrogen catabolite repression. This was confirmed by the reduction of hydantoin-hydrolysis in cells grown in excess carbon as opposed to nitrogen. Identification of a putative CRP-binding site within the promoter region of these enzymes further supported the regulatory role of carbon catabolite repression (CCR). As CCR in Pseudomonads is poorly understood, elucidation of the mechanism by which the hydantoinhydrolysing pathway in RU-KM3S is regulated would provide valuable insight into this complex process.
- Full Text:
- Date Issued: 2005
An investigation of the isolation, characterisation and application of hydantoinases for the industrial production of amino acids
- Authors: Kirchmann, Shaun
- Date: 2003
- Subjects: Hydantoin Amino acids Hydrolysis
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3969 , http://hdl.handle.net/10962/d1004028
- Description: This thesis describes a series of investigations into the hydantoin-hydrolysing activity of bacterial strains RU-KM1 and RU-OR, which were previously isolated for their ability to hydrolyse hydantoins to amino acids. The main aim of the study was to develop biotransformations with potential application in the production of enantiomerically pure amino acids using a bioreactor based system utilising the hydantoin hydrolysing enzymes of the two isolated microorganisms. Different substituted hydantoins may be used as substrates by these enzymes for the production of a variety of amino acids. These are not only important for amino acid production, but they may be used for production of other industrially important compounds, such as semisynthetic penicillin/ampicillin, L-aspartame (sweetener), Fluvalinate (insecticide), Enalapril (ACE inhibitor). Thus, the ability of the above-mentioned strains to hydrolyse these substrates was investigated, with the view to utilizing the maximum potential of these biocatalysts. Hydantoin conversion involves a two-step hydrolysis reaction which yields, initially, an N-carbamylamino acid intermediate, and subsequently, an amino acid. The hydantoin-hydrolysing enzymes of a Pseudomonas sp. RU-KM1, and an Agrobacterium sp. RU-OR were characterised as whole cells and in a crude extract preparation, and reaction conditions for its biocatalytic application were optimised. The optimum conditions for conversion of hydantoin to glycine were found to be 1 hour at 40 °C, with conversion yields greater than 30 % achieved. The enzymes of RU-KM1 demonstrated considerable stability, retaining 80 % of their activity after storage for 2 weeks at 4 °C. The activities of the enzymes were increased by the addition of a detergent to the extraction medium, suggesting that the enzymes might be membrane-bound. The results of the determination of the metal-dependence of the hydantoinase and N-carbamoylase of RU-KM1 suggested that these enzymes required metal ions for activity, with metal ions such as Cu[superscript (2+)], Fe[superscript (2+)], and Co[superscript (2+)] resulting in no significant change in enzyme activity, however there was an activation of the enzymes when Mn[superscript (2+)] was added to the enzymes. The stereoselectivity of the enzymes was investigated, and the results suggested that the hydantoinase was D-selective, whereas the N-carbamoylase was shown to be L-selective by other researchers. The hydantoin substrate selectivity of RU-KM1 and RU-OR was investigated, and the organisms were shown to be able to hydrolyse all of the seven substrates tested. However, there was a difference in activity levels between crude extract preparations and whole cells, with crude extracts generally showing slightly lower activity than whole cells in RU-KM1, and the whole cells or RU-OR showing the lower activity than its crude extract. Some difference was also observed in the order of preference of substrates between whole cells and crude extracts. The preferred substrate for RU-KM1 whole cells was isopropylhydantoin, whereas the crude extract preparation preferentially hydrolysed p-hydroxyphenylhydantoin, achieving 57 % and 52 % conversions respectively. RU-OR whole cells preferred methylhydantoin where as the crude extract preferred isopropylhydantoin, and showed 49 % and 51 % conversions respectively. The enzymes were characterised in terms of their temperature and pH optima, inducer requirements, and product inhibition studies. The hydantoinase of RU-KM1 was shown to be inducible with low levels of hydantoin, and thermostable upto 75 °C with its optima between 60 and 70 °C. The N-carbamoylase was shown to have its optima at 50 °C. The addition of ATP (0.5 mM), DTT (1 mM) and a protease inhibitor (2 mg.mL[superscript (-1)]) all increased the hydantoinase activity of RU-KM1 crude extract, however they had very little effect on the N-carbamoylase activity. The hydantoinase enzyme from extracts of RU-KM1 was partially purified by development of cell disruption methods using mechanical and lysing enzymes, followed by precipitation and chromatographic resolution. The results obtained showed a hydantoinase enzyme of between 48 and 66 kDa. RU-KM1 was grown under fermentation conditions using different minimal media. The activity and yields under these conditions were low. Previous attempt to grow the organism in a rich medium had resulted in an increase in biomass but no hydantoinase activity. A rich medium was developed by carbon and nitrogen optimisation and yielded biomass up to 30 g.L[superscript (-1)] dry cell weight. The hydantoinase activity was restored by nitrogen starvation in stationary phase. This resulted in high biomass with increased activity. This data is currently in press. Crude extract and whole cells were immobilised on flat sheet membranes, hollow fibre membranes and in alginate beads. Low hydantoinase activity was measured in bioreactors using membranes in different configurations. A significant increase in hydantoinase activity was measured when the crude extract was immobilised in sodium alginate, as a result of stabilisation of the N-carbamoylase. Temperature and pH optima were unaffected by the immobilisation procedure, however the durability of the enzymes increased 2-fold. Different configurations of the bioreactor were investigated, as well as a hydroxyphenylhydantoin as an alternative substrate in this study. The bioreactors showed a near 95 % conversion of the hydantoin to glycine, and a 99 % conversion using HPG. In conclusion, the hydantoin-hydrolysing enzymes of RU-KM1 have been shown to be possibly membrane associated, which is a novel finding. This study has shown that the hydantoinase of RU-KM1 is D-stereoselective, with high temperature stability. A growth medium was developed for the rapid production of active biomass. A bioreactor was developed using a single and a dual biocatalyst configuration, which was capable of hydrolysing hydantoin and monosubstituted hydantoins to produce amino acids. To our knowledge this system is the first such dual biocatalyst system reported for the production of amino acids.
- Full Text:
- Date Issued: 2003
- Authors: Kirchmann, Shaun
- Date: 2003
- Subjects: Hydantoin Amino acids Hydrolysis
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:3969 , http://hdl.handle.net/10962/d1004028
- Description: This thesis describes a series of investigations into the hydantoin-hydrolysing activity of bacterial strains RU-KM1 and RU-OR, which were previously isolated for their ability to hydrolyse hydantoins to amino acids. The main aim of the study was to develop biotransformations with potential application in the production of enantiomerically pure amino acids using a bioreactor based system utilising the hydantoin hydrolysing enzymes of the two isolated microorganisms. Different substituted hydantoins may be used as substrates by these enzymes for the production of a variety of amino acids. These are not only important for amino acid production, but they may be used for production of other industrially important compounds, such as semisynthetic penicillin/ampicillin, L-aspartame (sweetener), Fluvalinate (insecticide), Enalapril (ACE inhibitor). Thus, the ability of the above-mentioned strains to hydrolyse these substrates was investigated, with the view to utilizing the maximum potential of these biocatalysts. Hydantoin conversion involves a two-step hydrolysis reaction which yields, initially, an N-carbamylamino acid intermediate, and subsequently, an amino acid. The hydantoin-hydrolysing enzymes of a Pseudomonas sp. RU-KM1, and an Agrobacterium sp. RU-OR were characterised as whole cells and in a crude extract preparation, and reaction conditions for its biocatalytic application were optimised. The optimum conditions for conversion of hydantoin to glycine were found to be 1 hour at 40 °C, with conversion yields greater than 30 % achieved. The enzymes of RU-KM1 demonstrated considerable stability, retaining 80 % of their activity after storage for 2 weeks at 4 °C. The activities of the enzymes were increased by the addition of a detergent to the extraction medium, suggesting that the enzymes might be membrane-bound. The results of the determination of the metal-dependence of the hydantoinase and N-carbamoylase of RU-KM1 suggested that these enzymes required metal ions for activity, with metal ions such as Cu[superscript (2+)], Fe[superscript (2+)], and Co[superscript (2+)] resulting in no significant change in enzyme activity, however there was an activation of the enzymes when Mn[superscript (2+)] was added to the enzymes. The stereoselectivity of the enzymes was investigated, and the results suggested that the hydantoinase was D-selective, whereas the N-carbamoylase was shown to be L-selective by other researchers. The hydantoin substrate selectivity of RU-KM1 and RU-OR was investigated, and the organisms were shown to be able to hydrolyse all of the seven substrates tested. However, there was a difference in activity levels between crude extract preparations and whole cells, with crude extracts generally showing slightly lower activity than whole cells in RU-KM1, and the whole cells or RU-OR showing the lower activity than its crude extract. Some difference was also observed in the order of preference of substrates between whole cells and crude extracts. The preferred substrate for RU-KM1 whole cells was isopropylhydantoin, whereas the crude extract preparation preferentially hydrolysed p-hydroxyphenylhydantoin, achieving 57 % and 52 % conversions respectively. RU-OR whole cells preferred methylhydantoin where as the crude extract preferred isopropylhydantoin, and showed 49 % and 51 % conversions respectively. The enzymes were characterised in terms of their temperature and pH optima, inducer requirements, and product inhibition studies. The hydantoinase of RU-KM1 was shown to be inducible with low levels of hydantoin, and thermostable upto 75 °C with its optima between 60 and 70 °C. The N-carbamoylase was shown to have its optima at 50 °C. The addition of ATP (0.5 mM), DTT (1 mM) and a protease inhibitor (2 mg.mL[superscript (-1)]) all increased the hydantoinase activity of RU-KM1 crude extract, however they had very little effect on the N-carbamoylase activity. The hydantoinase enzyme from extracts of RU-KM1 was partially purified by development of cell disruption methods using mechanical and lysing enzymes, followed by precipitation and chromatographic resolution. The results obtained showed a hydantoinase enzyme of between 48 and 66 kDa. RU-KM1 was grown under fermentation conditions using different minimal media. The activity and yields under these conditions were low. Previous attempt to grow the organism in a rich medium had resulted in an increase in biomass but no hydantoinase activity. A rich medium was developed by carbon and nitrogen optimisation and yielded biomass up to 30 g.L[superscript (-1)] dry cell weight. The hydantoinase activity was restored by nitrogen starvation in stationary phase. This resulted in high biomass with increased activity. This data is currently in press. Crude extract and whole cells were immobilised on flat sheet membranes, hollow fibre membranes and in alginate beads. Low hydantoinase activity was measured in bioreactors using membranes in different configurations. A significant increase in hydantoinase activity was measured when the crude extract was immobilised in sodium alginate, as a result of stabilisation of the N-carbamoylase. Temperature and pH optima were unaffected by the immobilisation procedure, however the durability of the enzymes increased 2-fold. Different configurations of the bioreactor were investigated, as well as a hydroxyphenylhydantoin as an alternative substrate in this study. The bioreactors showed a near 95 % conversion of the hydantoin to glycine, and a 99 % conversion using HPG. In conclusion, the hydantoin-hydrolysing enzymes of RU-KM1 have been shown to be possibly membrane associated, which is a novel finding. This study has shown that the hydantoinase of RU-KM1 is D-stereoselective, with high temperature stability. A growth medium was developed for the rapid production of active biomass. A bioreactor was developed using a single and a dual biocatalyst configuration, which was capable of hydrolysing hydantoin and monosubstituted hydantoins to produce amino acids. To our knowledge this system is the first such dual biocatalyst system reported for the production of amino acids.
- Full Text:
- Date Issued: 2003
The governance and management of commonages in three small towns in the Eastern Cape, South Africa
- Authors: Martens, Claire
- Date: 2009
- Subjects: Commons -- Conservation -- South Africa -- Eastern Cape Natural resources, Communal -- Management -- South Africa -- Eastern Cape Rural development -- South Africa -- Eastern Cape Land tenure -- South Africa Land reform -- South Africa Property -- South Africa Property rights -- South Africa
- Language: English
- Type: Thesis , Masters , MA
- Identifier: vital:4757 , http://hdl.handle.net/10962/d1007142
- Description: Commonage is land that is usually found adjacent to a town, which is owned by the local municipality and acquired through state grants or, historically, through the church. Since the new government dispensation in 1994, poor and previously disadvantaged residents have acquired access rights to commonage for agricultural purposes. Through the Department of Land Affair’s Commonage Programme, local municipalities are acquiring more commonage land for purposes of agriculture and grazing livestock. Commonages are increasingly being recognised as an important livelihood asset for the poor and unemployed residents’ of towns and rapid urbanisation is contributing to the increasing use of commonage for livelihood provisioning. Some municipalities view commonage as a key asset to promote Local Economic Development, while others are finding it difficult to manage the land effectively, to the extent that some analysts see tragic ecological consequences occurring due to over-grazing. This has been likened to the “tragedy of the commons” as advocated by Hardin in 1968. Commonage and common property resource systems have many similarities and co-management has been advocated as a potential management regime for commonage. Researching the policy framework, institutional structures and management bodies involved in commonage, gave a better understanding of the governance and management of the commonages in Grahamstown, Fort Beaufort and Bathurst. Current management attempts are not ensuring the efficient, equitable and sustainable use of these commonages. The governance framework is not adequately supporting proper management. In an environment of resource-poor institutional bodies, adaptive co-management could prove to be the most effective system to ensure the sustainable use and development of this natural resource. Furthermore, commonage is no longer contributing to the Land Reform Programme. Commonage should be better integrated into agrarian reform through lease schemes and an efficient Emerging Farmer Programme.
- Full Text:
- Date Issued: 2009
- Authors: Martens, Claire
- Date: 2009
- Subjects: Commons -- Conservation -- South Africa -- Eastern Cape Natural resources, Communal -- Management -- South Africa -- Eastern Cape Rural development -- South Africa -- Eastern Cape Land tenure -- South Africa Land reform -- South Africa Property -- South Africa Property rights -- South Africa
- Language: English
- Type: Thesis , Masters , MA
- Identifier: vital:4757 , http://hdl.handle.net/10962/d1007142
- Description: Commonage is land that is usually found adjacent to a town, which is owned by the local municipality and acquired through state grants or, historically, through the church. Since the new government dispensation in 1994, poor and previously disadvantaged residents have acquired access rights to commonage for agricultural purposes. Through the Department of Land Affair’s Commonage Programme, local municipalities are acquiring more commonage land for purposes of agriculture and grazing livestock. Commonages are increasingly being recognised as an important livelihood asset for the poor and unemployed residents’ of towns and rapid urbanisation is contributing to the increasing use of commonage for livelihood provisioning. Some municipalities view commonage as a key asset to promote Local Economic Development, while others are finding it difficult to manage the land effectively, to the extent that some analysts see tragic ecological consequences occurring due to over-grazing. This has been likened to the “tragedy of the commons” as advocated by Hardin in 1968. Commonage and common property resource systems have many similarities and co-management has been advocated as a potential management regime for commonage. Researching the policy framework, institutional structures and management bodies involved in commonage, gave a better understanding of the governance and management of the commonages in Grahamstown, Fort Beaufort and Bathurst. Current management attempts are not ensuring the efficient, equitable and sustainable use of these commonages. The governance framework is not adequately supporting proper management. In an environment of resource-poor institutional bodies, adaptive co-management could prove to be the most effective system to ensure the sustainable use and development of this natural resource. Furthermore, commonage is no longer contributing to the Land Reform Programme. Commonage should be better integrated into agrarian reform through lease schemes and an efficient Emerging Farmer Programme.
- Full Text:
- Date Issued: 2009
Rhodeo, Vol. 22, No. 16
- Date: 1968-08-22
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14590 , http://hdl.handle.net/10962/d1019462
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-08-22
- Date: 1968-08-22
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14590 , http://hdl.handle.net/10962/d1019462
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-08-22
King Kong: gala preview in aid of the African Music and Drama Trust
- Authors: Goldreich, Arhtur
- Date: 1959
- Subjects: King Kong (Musical) -- History and critisism , Musicals -- South Africa -- History and critisism , Music -- South Africa , Matshikiza, Todd, 1921-1968 -- King Kong
- Language: English
- Type: text
- Identifier: http://hdl.handle.net/10962/53867 , vital:26340 , This image is held at the Cory Library for Humanities Research at Rhodes University. For further information contact cory@ru.ac.za. The digitisation of this image was made possible through a generous grant received from the Andrew W. Mellon Foundation 2014-2017.
- Full Text:
- Date Issued: 1959
- Authors: Goldreich, Arhtur
- Date: 1959
- Subjects: King Kong (Musical) -- History and critisism , Musicals -- South Africa -- History and critisism , Music -- South Africa , Matshikiza, Todd, 1921-1968 -- King Kong
- Language: English
- Type: text
- Identifier: http://hdl.handle.net/10962/53867 , vital:26340 , This image is held at the Cory Library for Humanities Research at Rhodes University. For further information contact cory@ru.ac.za. The digitisation of this image was made possible through a generous grant received from the Andrew W. Mellon Foundation 2014-2017.
- Full Text:
- Date Issued: 1959
Rhodeo, Vol. 22, No. 17
- Date: 1968-08-29
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14591 , http://hdl.handle.net/10962/d1019463
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-08-29
- Date: 1968-08-29
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14591 , http://hdl.handle.net/10962/d1019463
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-08-29
Rhodeo, Vol. 22, No. 13
- Date: 1968-06-13
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14587 , http://hdl.handle.net/10962/d1019459
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-06-13
- Date: 1968-06-13
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14587 , http://hdl.handle.net/10962/d1019459
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1968-06-13
Rhodeo, Vol. 22, No. 8
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14583 , http://hdl.handle.net/10962/d1019455
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14583 , http://hdl.handle.net/10962/d1019455
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
Rhodes University Graduation Ceremony 1994
- Authors: Rhodes University
- Date: 1994
- Language: English
- Type: text
- Identifier: vital:8128 , http://hdl.handle.net/10962/d1006753
- Description: Rhodes University Graduation Ceremonies Friday, 8 April 1994 at 10:30 a.m. [and] 08:15 p.m. [and] Saturday, 9 April 1994 at 10:30 a.m. in the 1820 Settlers National Monument. , Rhodes University East London Graduation Ceremony Saturday, 14 May 1994 at 11.00 a.m. in the Guild Theatre.
- Full Text:
- Date Issued: 1994
- Authors: Rhodes University
- Date: 1994
- Language: English
- Type: text
- Identifier: vital:8128 , http://hdl.handle.net/10962/d1006753
- Description: Rhodes University Graduation Ceremonies Friday, 8 April 1994 at 10:30 a.m. [and] 08:15 p.m. [and] Saturday, 9 April 1994 at 10:30 a.m. in the 1820 Settlers National Monument. , Rhodes University East London Graduation Ceremony Saturday, 14 May 1994 at 11.00 a.m. in the Guild Theatre.
- Full Text:
- Date Issued: 1994
Rhodes University Graduation Ceremony 1992
- Authors: Rhodes University
- Date: 1992
- Language: English
- Type: text
- Identifier: vital:8126 , http://hdl.handle.net/10962/d1006751
- Description: Rhodes University Graduation Ceremonies Friday, 10 April 1992 at 10:30 a.m. [and] 08:15 p.m. [and] Saturday, 11 April 1992 at 10:30 a.m. in the 1820 Settlers National Monument. , Rhodes University East London Graduation Ceremony Saturday, 16 May 1992 at 11:00 a.m. in the Guild Theatre.
- Full Text:
- Date Issued: 1992
- Authors: Rhodes University
- Date: 1992
- Language: English
- Type: text
- Identifier: vital:8126 , http://hdl.handle.net/10962/d1006751
- Description: Rhodes University Graduation Ceremonies Friday, 10 April 1992 at 10:30 a.m. [and] 08:15 p.m. [and] Saturday, 11 April 1992 at 10:30 a.m. in the 1820 Settlers National Monument. , Rhodes University East London Graduation Ceremony Saturday, 16 May 1992 at 11:00 a.m. in the Guild Theatre.
- Full Text:
- Date Issued: 1992
Grahamstown : average number of rooms per dwelling
- Authors: Watts, Hilstan Lett, 1929-
- Date: 1957
- Subjects: f-sa , 2 cm = 2000 yards 30.5595° S, 22.9375° E , Grahamstown (South Africa) Maps , Grahamstown (South Africa) Street maps , South Africa History 1909-1961 , South Africa History 1836-1909
- Language: English
- Type: maps , digital maps , cartographic
- Identifier: http://hdl.handle.net/10962/121281 , vital:34995 , Cory Library for Humanities Research, Rhodes University Library, Grahamstown, South Africa , T654_22
- Description: Map 22 in the map album accompanying the thesis by Hilstan Lett Watts, "Grahamstown : a socio-ecological study of a small South African town", Rhodes University thesis, 1957. Map signed 1955. The data are based on mean values calculated for each street, using survey sample data for the number of rooms per dwelling.
- Full Text: false
- Date Issued: 1957
- Authors: Watts, Hilstan Lett, 1929-
- Date: 1957
- Subjects: f-sa , 2 cm = 2000 yards 30.5595° S, 22.9375° E , Grahamstown (South Africa) Maps , Grahamstown (South Africa) Street maps , South Africa History 1909-1961 , South Africa History 1836-1909
- Language: English
- Type: maps , digital maps , cartographic
- Identifier: http://hdl.handle.net/10962/121281 , vital:34995 , Cory Library for Humanities Research, Rhodes University Library, Grahamstown, South Africa , T654_22
- Description: Map 22 in the map album accompanying the thesis by Hilstan Lett Watts, "Grahamstown : a socio-ecological study of a small South African town", Rhodes University thesis, 1957. Map signed 1955. The data are based on mean values calculated for each street, using survey sample data for the number of rooms per dwelling.
- Full Text: false
- Date Issued: 1957
- Authors: Andrew
- Identifier: http://hdl.handle.net/10962/226990 , vital:49397
- Full Text: false
Rhodeo, Vol. 16, No. 10
- Date: 1962-08-22
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14470 , http://hdl.handle.net/10962/d1019342
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1962-08-22
- Date: 1962-08-22
- Subjects: Grahamstown -- Newspapers , Journalism, Students -- South Africa , Rhodes University -- Activate , Rhodes University -- Students , Student newspapers and periodicals -- South Africa
- Language: English
- Type: Text
- Identifier: vital:14470 , http://hdl.handle.net/10962/d1019342
- Description: Rhodeo is the Independent Student Newspaper of Rhodes University. Located in Grahamstown, Rhodeo was established in 1947, and renamed in 1994 as Activate. During apartheid Rhodeo became an active part of the struggle for freedom of expression as part of the now defunct South African Student Press Union. Currently Activate is committed to informing Rhodes University students, staff and community members about relevant issues, mainly on campus. These issues range from hard news to more creative journalism. While Activate acts as a news source, one of its main objectives it to be accessible as a training ground for student journalists. The newspaper is run entirely by the students and is published twice a term. Activate is a free newspaper which receives an annual grant from the Rhodes University Student Representative Council, however, majority of its revenue is generated through advertising.
- Full Text:
- Date Issued: 1962-08-22
Xhosa dance with marimbas
- Marimba Group, Composer Not Specified, Dargie, Dave
- Authors: Marimba Group , Composer Not Specified , Dargie, Dave
- Date: 1988
- Subjects: Folk music , Music--Religious aspects , Field recordings , Africa, Sub-Saharan , Europe Germany Munich gw
- Language: isiXhosa
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/316962 , vital:59885 , International Library of African Music, Rhodes University, Makhanda, South Africa , Dave Dargie Field Tapes, Rhodes University, Makhanda, South Africa , DD140-22
- Description: Religious dance song with clapping, rattles and Marimba accompaniment.
- Full Text: false
- Date Issued: 1988
- Authors: Marimba Group , Composer Not Specified , Dargie, Dave
- Date: 1988
- Subjects: Folk music , Music--Religious aspects , Field recordings , Africa, Sub-Saharan , Europe Germany Munich gw
- Language: isiXhosa
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/316962 , vital:59885 , International Library of African Music, Rhodes University, Makhanda, South Africa , Dave Dargie Field Tapes, Rhodes University, Makhanda, South Africa , DD140-22
- Description: Religious dance song with clapping, rattles and Marimba accompaniment.
- Full Text: false
- Date Issued: 1988
Modemo o lerato
- Composer Not Specified, St Rose's Parish, Dargie, Dave
- Authors: Composer Not Specified , St Rose's Parish , Dargie, Dave
- Date: 1982-08-22
- Subjects: Choral music , Field recordings , Africa, Sub-Saharan , Africa South Africa Bloemfontein f-sa
- Language: Southern Sotho
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/274473 , vital:54929 , International Library of African Music, Rhodes University, Makhanda, South Africa , Dave Dargie Field Tapes, Rhodes University, Makhanda, South Africa , DD051-22
- Description: Adaptation of Church Song.
- Full Text: false
- Date Issued: 1982-08-22
- Authors: Composer Not Specified , St Rose's Parish , Dargie, Dave
- Date: 1982-08-22
- Subjects: Choral music , Field recordings , Africa, Sub-Saharan , Africa South Africa Bloemfontein f-sa
- Language: Southern Sotho
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/274473 , vital:54929 , International Library of African Music, Rhodes University, Makhanda, South Africa , Dave Dargie Field Tapes, Rhodes University, Makhanda, South Africa , DD051-22
- Description: Adaptation of Church Song.
- Full Text: false
- Date Issued: 1982-08-22
Akweni (Sister I am tired)
- Authors: Chewa women , Hugh Tracey
- Date: 1958
- Subjects: Folk music--Africa , Field recordings , Songs, Nyanja , Songs, Chewa , Nyanja (African people) , Chewa (African people) , Folk music , Africa Malawi Chadza, Lilongwe District, Nyasaland f-mw
- Language: Nyanja, Chewa, Chichewa
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/153509 , vital:39460 , International Library of African Music, Rhodes University, Grahamstown, South Africa , TR076-22
- Description: The woman reports to her sister-in-law that her husband is not good as he beats her every day. Pounding song with pestle and mortar.
- Full Text: false
- Date Issued: 1958
- Authors: Chewa women , Hugh Tracey
- Date: 1958
- Subjects: Folk music--Africa , Field recordings , Songs, Nyanja , Songs, Chewa , Nyanja (African people) , Chewa (African people) , Folk music , Africa Malawi Chadza, Lilongwe District, Nyasaland f-mw
- Language: Nyanja, Chewa, Chichewa
- Type: sound recordings , field recordings , sound recording-musical
- Identifier: http://hdl.handle.net/10962/153509 , vital:39460 , International Library of African Music, Rhodes University, Grahamstown, South Africa , TR076-22
- Description: The woman reports to her sister-in-law that her husband is not good as he beats her every day. Pounding song with pestle and mortar.
- Full Text: false
- Date Issued: 1958