An investigation of the effetiveness of correctional centre-based vocational training programmes towards reducing recidivism
- Authors: Mangesi, Nosipho
- Date: 2019
- Subjects: Recidivism Social justice
- Language: English
- Type: Thesis , Masters , MSoc (Criminology)
- Identifier: http://hdl.handle.net/10353/16408 , vital:40717
- Description: Since the Department of Correctional Services has been transformed into an institution of rehabilitation and skills development, there is a need for a sound classification system whereby offenders are classified according to their potential for treatment and training programmes that match their risk/needs. The study was conducted in Middledrift Correctional Centre in the Eastern Cape with the aim of examining the effectiveness of correctionally based vocational training programmes towards reducing recidivism. Research towards correctional programmes was necessitated by the extant of recidivism in South Africa. The question is where does the problem lie because offenders are provided with rehabilitation programmes to make them law abiding citizens and reintegrate well into the community up on release but, in many cases it does not become possible as many ex-offenders return to custody either for new offence or parole violation. The study used qualitative design in data collection and in explaining the results. A sample of sixteen recidivists and five correctional officials formed participants for the study selecting using purposive sampling procedures. Involvement in vocational programmes was used as a criteria for selectiong of correctional officials as participants. In-depth interviews were conducted with eight recidivists and all five correctional officials and a focus group interview was held with the other eight set of recidivists. The study examined the impact of vocational programmes on recidivism followed by the factors that hinder effective offender rehabilitation and factors that influence recidivism up on release. The findings of this study were analysed using thematic analysis with the assistance of a voice recorder as a back up for collected data. Findings revealed that a small number of recidivists attend vocational training programmes and these programmes vi (vocational) are short in the centre together with programme facilitators at the time of reporting. Offenders stated that the available vocational programmes are of no interest to them. Participantas stated that vocational training does assist in desisting criminal activities up on release as it provide skills and opportunities for employment to curb unemployment as indicated as a major factor influencing recidivism. Findings also revealed that periodic re-assesment is not adequately conducted and classification for vocational training is not likely to be sufficiently done according to offender risk/needs. The study recommends that, a large number of offenders be provided with vocational training programmes and that offender classification incorporate the principles of RNR model
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- Date Issued: 2019
Bioinformatic analysis, isolation and kinetic characterisation of red algae (Gelidium capense) dehydrogenases
- Authors: Gogela, Yanga
- Date: 2019
- Subjects: Bioinformatics Chondrus crispus
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: http://hdl.handle.net/10353/19164 , vital:39878
- Description: Lactate and alcohol dehydrogenases have attracted much attention in various industries and scientific research for their ability to produce chirally pure compounds and be assayed for activity using more straightforward and reproducible assay methods. These enzymes have been previously isolated and purified from various plants, animals and microorganisms. So far, the molecular and biochemical properties of enzymes from these dehydrogenase families in red algae are mostly unknown. Red macroalgae have been used for centuries for the treatment of various diseases and as a source of ingredients in the food industry. The aim of this study was to identify genes in the sequenced red algae genomes that encode dehydrogenases, to use bioinformatic tools to confirm that the proteins encoded are dehydrogenases and to isolate and kinetically purify alcohol or lactate dehydrogenase from red algae species found along the coastline of the Eastern Cape Province. A combination of bioinformatics tools, molecular and biochemical techniques were used to identify, purify, and characterise ADH and LDH enzymes. Bioinformatics analysis revealed two alcohol dehydrogenase genes and two hypothetical genes encoding functional domains similar to D-lactate dehydrogenases from other species. The ADH and LDH-like genes shared low sequence identity at the protein level with medium-chain dehydrogenases/reductases (MDRs) and 2-hydroxy acid dehydrogenases, respectively. These two dehydrogenase genes showed a highly conserved NAD-binding motif (Rossmann-fold) similar to many other NAD-dependent dehydrogenases. The ADH and LDH proteins contained no signal peptides and may be located in the cytoplasm. The phylogenetic tree analysis showed that the two ADH genes belonged to cinnamyl and class III alcohol dehydrogenases, whereas the LDHlike genes were grouped with D-lactate dehydrogenases from other organisms. The ADH and LDH gene family showed cis-acting regulatory elements that are mostly involved in stress response and hormonal response. Structural analysis showed that the dehydrogenases 3D structure predicted models comprise of two domains, namely the substrate binding and the coenzyme binding domains that are rich in beta-strands secondary structure elements. The LDH from red algae was purified approximately 4-fold with a specific activity of 0.044 U/mg. The purified LDH enzyme had a molecular weight of approximately 37kDa. The LDH was active across a broad pH range from 5-9 with a pH optimum observed at 7.5. The LDH ii enzyme in red algae exhibits a temperature optimum of 40 ⁰C and heat stability up to 40 ⁰C. Above 50 °C the LDH activity rapidly decreased showing that the LDH in red algae is not thermostable. The LDH enzyme showed a Km value of 0.8 mM and Vmax of 0.0067 mM.min-1 when using sodium pyruvate as a substrate.
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- Date Issued: 2019