: the representation of rape in Lewis Nkosi’s Mating Birds and Arthur Maimane’s Hate No More
- Authors: Yawa, Sibulele Yola
- Date: 2021-02
- Subjects: South Africa--Politics and government--1994 , Post-apartheid era--South Africa
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/21134 , vital:47131
- Description: The main aim of this thesis is to provide a literary study through a comparative analysis of how sexual politics are played out in the texts Mating Birds by Lewis Nkosi and Hate No More by Arthur Maimane. It seeks to determine the modalities of representation of rape in each text and also to investigate the extent to which the novels are similar or different in the way in which they represent sexual politics or the politics of rape during the apartheid era. This investigation was done using Frantz Fanon‟s postcolonial theory and, particularly, his seminal work, Black Skin, White Masks. Most importantly, for the purpose of this study, is Fanon‟s chapter on the love/sexual relationships between the man of colour and the white woman. This is helpful as Fanon touches on what he believes the attraction of the man of colour to the white woman stems from. Using Fanon‟s theory, one discovers that the motivation for Ndi Sibiya to allegedly rape Veronica stems from his anger at the system of apartheid and its oppression of black people. This is similar to Philip Mokone‟s case; the novel explicitly states that he was motivated by anger and his rape of Jean Ryan was a form of communication to the white people and the apartheid system. , Thesis (MA) (English) -- University of Fort Hare, 2021
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- Date Issued: 2021-02
Adolescent sexual reproductive health and rights in the Alice area, Eastern Cape Province of South Africa
- Authors: Moko, Zukhanye
- Date: 2021-02
- Subjects: Reproductive health , Right to health , HIV infections
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20676 , vital:46423
- Description: Sexual Reproductive Health (SRH) is a significant aspect of adolescent’s growth. Adolescents particularly girls face the risk of exposure to Human Immunodeficiency Virus (HIV), Sexually Transmitted Diseases (STDs), child marriages, high rates of unwanted pregnancy and the risk of those pregnancies can lead to unsafe abortion. In South Africa, considerable progress has been made in achieving improved access to Sexual Reproductive Health and Rights (SRHR) among the general population, however, some factors influencing SRHR of adolescents and young people have been slow to achieve. The study aims to investigate factors influencing Sexual Reproductive Health and Rights of adolescents in Alice, which is located in the Eastern Cape Province of South Africa. The Social-Ecological Model was considered appropriate for this study as it provides a comprehensive understanding of the multiple and interacting determinants of Sexual Reproductive Health and Rights. A qualitative methodology was adopted, involving focus groups with high school learners, in-depth interviews with institutional actors (Department of Health, Basic Education and Social Development), and participant observations. The study reveals that adolescents’ have access to Sexual Reproductive Health services from healthcare centres but only a few utilize or access them due to barriers such as the geographical location, denial and judgement about young people's sexuality limits their access to comprehensive knowledge to protect and promote their Sexual and Reproductive Health. The findings show that the adolescents who were most affected by Sexual Reproductive Health and Rights challenges were those from deep rural areas. They had minimal information/education compared to those residing in areas close to the town of Alice and major roads. Multi-sectoral interventions empowering adolescents and young people to exercise their rights to optimize SRHR service yield better results. , Thesis (MSc) -- Faculty of Science & Agriculture, 2021
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- Date Issued: 2021-02
An analysis of students’ constructions of the ‘fees must Fall’ movement at an historically black university
- Authors: Chandler, Kelly Jean
- Date: 2021-02
- Subjects: Student movements , College students--Political activity , Student protesters
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/21058 , vital:46939
- Description: The ‘Fees Must Fall’ movement which occured in 2015 and 2016 was a major national event which affected most higher education institutions in South Africa. This research considers the constructions of the ‘Fees Must Fall’ movement at an historically black university, namely, the University of Fort Hare. Furthermore, the research analyzes how students are positioned in their constructions in relation to the movement. The study aims to contribute to the understanding of the lived experiences of student activists in the 2015 and 2016 ‘Fees Must Fall’ movement at the University of Fort Hare. The data collection method used was a convenience sampling method with seven participants interviewed. Making use of the guidelines of a Foucauldian Discourse Analysis, four primary discourses were identified from the data collected: coercion discourses; fear discourses; financial discourses; and meritocracy discourses. The positions of students were varied and consisted of both agentic and submissive positions, with the student representative council frequently being positioned dominantly. The theoretical framework also included Michel Foucault’s theories of governmentality and biopower which contributed significantly to the understandings of institutional power in the university context. The research is conducted against ethical backdrop of the philosophies and guidelines of postcolonial psychology. The broader context of South Africa is observed and discussed, specifically recognizing the legacy of apartheid and other historical antecedents such as colonization. The issues of transformation, institutional racism, and decolonization are placed at the forefront of this research endeavour. , Thesis (MSoc Sci) (Psychology) - - University of Fort Hare, 2021
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- Date Issued: 2021-02
Bioconversion of chicken feather into amino acids and keratinase production by mesophilic Chryseobacterium proteolyticum and Pseudomonas aeruginosa isolated from municipal waste dumpsites
- Authors: Giwu, Nonkonzo https://orcid.org/0000-0001-9416-7896
- Date: 2021-02
- Subjects: Poultry -- Processing , Proteolytic enzymes
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/22732 , vital:52720
- Description: Chicken feathers are by-products of poultry processing which are generated in large amount because of the global growing demand for poultry meats. They have high contents of crude proteins in the form of keratin which could be valorized into digestible products. Keratinases are classified as a specific collection of proteolytic enzymes that have the ability for the degradation of recalcitrant keratinous substrates. Isolation and characterization of these enzymes from various microbial producers are gaining prominence in recent years due to their industrial and biotechnological application potentials. For this research, the collection of soil samples was done as well as the isolation of bacteria and the screening for keratinolytic activity. 16S rDNA sequencing and phylogenetic analysis were used to identify the isolates with efficient chicken feathers degrading capacity. Optimum conditions for the fermentation prcocess was enhanced for the production of keratinase. The fermentation broth was also analysed for various amino acids of protein, and the biochemical properties of the enzymes were likewise determined. Twenty two (22) bacteria were isolated from the soil samples, and 18 out of the 22 isolates showed proteolytic activity on solid media with diameters of halo zone that ranged from 5 ± 0.71 mm for isolate coded as PSS-03 to 25 ± 1.41 mm for isolate coded as PSS-06. Intact chicken feathers were degraded by proteolytic bacterial isolates in variable degree that ranged from 24percent for PSS-10 and 81percent for DSS-02. Extracellular keratinase production recorded for the isolates ranged from 63.63 ± 4.14 U/mL for PSS-10 to 693.63 ± 62.99 U/mL for DSS-02. Based on 16S rDNA sequence and phylogenetic analysis, the 2 isolates with remarkable keratinolytic activity coded as DSS-02 and PSS-14 were identified as Chryseobacterium proteolyticum FGNn and Pseudomonas aeruginosa GNFx. C. proteolyticum showed the maximum keratinase production of 756.36 U/mL after 72 h of incubation at optimized fermentation conditions which involved initial medium pH (4), incubation temperature (30 oC), inoculum size (2percent; v/v), and chicken feathers (1.5percent; w/v). Similarly, P. aeruginosa optimally produced keratinase (1055.45 U/mL) after 96 h of incubation at optimized fermentation conditions that involved initial medium pH (7-8), incubation temperature (30 oC), inoculum size (5percent; v/v), and chicken feathers (2.5percent; w/v). Furthermore, feather hydrolysate from C. proteolyticum FGNn had relatively higher abundance (>1.5g/100g sample) of arginine (1.85), serine (1.63), glycine (1.9) and lysine (1.62); while P. aeruginosa GNFx feather hydrolysate showed high abundance of arginine, serine, aspartic acid, glutamic acid, glycine, alanine, valine, and leucine with respective concentration of 2.06, 1.67, 2.39, 3.05, 1.87, 1.73, 1.56 and 1.65 (g/100g sample). The results showed that keratinases from the two bacterial isolates were optimally active at pH 8, and temperature of 50 oC for FGNn keratinase and 50-60 oC for GNFx keratinase. The enzymes displayed remarkable pH stability. Keratinase from C. proteolyticum was catalytically inhibited by EDTA and 1,10-phenanthroline but not affected by PMSF; while P. aeruginosa keratinase was not significantly affected by those class of protease inhibitors. Adiitionally, FGNn keratinase demonstrated high residual activity of 90percent, 103percent, 101percent, 110percent, 130, and 105percent in the presence of DTT, hydrogen peroxides, acetonitrile, triton X-100, tween-80 and SDS, respectively. Similarly, catalytic efficiency of GNFx keratinase was promoted in the presence of hydrogen peroxides (119percent), triton X-100 (140percent), tween-80 (150percent) and SDS (147percent) compared to the control. Furthermore, the keratinases from the both bacterial isolates exhibited catalytic efficiency enhancement and remarkable structural stability in the presence of laundry detergents tested. The findings from the study suggest the application potentials of the isolates for the bioconversion of recalcitrant keratinous wastes into digestible and quality protein hydrolysates. The properties of these microbial keratinases indicate that they may be exploited for various biotechnological and industrial processes especially in the formulation of detergents. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
Chicken feather delipidation by lipolytic bacteria isolated from an aquatic environment
- Authors: Shiri, Tariro https://orcid.org/0000-0002-0290-9854
- Date: 2021-02
- Subjects: Keratin
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/21479 , vital:48693
- Description: Keratinous biomass contributes a significant proportion of agro-based wastes in the ecosystem with minimal potentials for valuable product recovery. The generation of huge quantities of chicken feather from poultry processing farms prompts the valorization attempt via diverse avenues. Chicken feathers are a rich source of valuable keratin, yet the overall value chain is rudimentary based on unsustainable recovery techniques involving corrosive chemicals and high energy input processes. Although attempts have been made to extract keratin using microbial techniques successfully, the pre-treatment stage remains dominated by chemical use. Chicken feathers are composed of approximately 91percent keratin, 1percent lipids, and 8percent water. Therefore, lipid removal is a critical step in the valorization process as they contribute to access hindrance of the keratinases and other sulfitolytic systems to keratin. Consequently, the study undertook to explore the environment for lipolytic bacteria capable of degrading chicken feathers' lipid components. Sediment samples were collected for bacteria isolation. The bacteria were evaluated for lipolytic activity, and the potent isolates were identified based on 16S rRNA gene sequencing. The fermentation conditions for the production of extracellular lipases were optimized, and the produced lipases were characterized. Lastly, chicken feather lipids were hydrolysed with lipolytic bacteria. Out of twenty bacteria isolated from the sediment samples, six isolates coded as ACT003, ACT004, ACT010, ACT013, ACT016, and ACT019 showed lipolytic activity on solid media with a respective diameter of 12 mm, 66 mm, 29 mm, 11 mm, 12 mm, and 10 mm. Based on 16S rRNA gene sequencing and phylogenetic analysis, the isolates coded as ACT004 and ACT010 were identified as Bacillus sp. TTs1 and Bacillus sp. TTs2; and the nucleotide sequences were submitted to GenBank (NCBI) with the accession numbers MW556206 and MW556207, respectively. Bacillus sp. TTs1 showed the maximum lipase production of 641.25 U/mL at 72 h, under optimized conditions that included initial pH (5), inoculum size (2percent, v/v), incubation temperature (45 oC), agitation speed (140 rpm), CaCl2 (0.01percent, w/v), yeast extract (1percent, w/v), and tween-80 (10percent, v/v). Similarly, the lipase production by Bacillus sp. TTs2 peaked at 96 h with enzyme activity of 618.8 U/mL in improved fermentation conditions consisting of initial pH (5), inoculum size (2-8percent, v/v), incubation temperature (25 oC), agitation speed (180 rpm), CaCl2 (0.01percent, w/v), yeast extract and peptone (1percent, w/v), and tween-80 (10percent, v/v). The evaluation of chicken feather concentrations on free fatty acid liberation showed that 6-8percent (w/v) chicken feather was adequate with free fatty acids contents of 0.58percent and 0.86percent for Bacillus sp. TTs1 and Bacillus sp. TTs2, respectively. Both isolates' lipases showed remarkable catalytic efficiency at pH and temperature of 7 and 40oC, respectively. The comparative analysis of residual lipids between pre-and post-fermentation indicated a 39.9 ± 7.8percent and 51.2 ± 20.2percent hydrolysis efficiency for Bacillus sp. TTs1 and Bacillus sp. TTs2, respectively. This study's findings indicated the lipolytic potentials of Bacillus spp. and suggest the possibility of a full bio-based approach for chicken feather lipid removal in the valorization of chicken feathers. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
Electrochemical sensing based on functionalised carbon dots prepared by bottom-up approach
- Authors: Madikizela, Ziyanda https://orcid.org/0000-0003-0405-8464
- Date: 2021-02
- Subjects: Electrochemical analysis , Electrodes, Carbon
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/22545 , vital:52424
- Description: This research was aimed at preparing carbon dots using the microwave method as a bottomup synthetic approach. The prepared carbon dots were them to be used as an electrode modifier in electrochemical detection of metal ion. The structure of the carbon dots prepared were characterized using different techniques including the FTIR, TEM, UV-Vis, PL, XRD and Raman Spectroscopy. It was observed that the nanoparticles consisted of carboxylic acid, amine and alcohol functional groups at their core and surface. UV-Vis and PL revealed that the carbon dots absorb more light in the visible and ultraviolet region, and the sizes of the carbon dots prepared were less than 10 nm. The carbon dots were then utilized for electrochemical sensing of Cd2+ ion, which is considered as one of harmful heavy metal ion when not controlled. Glassy carbon electrode modified with the carbon dots was utilized for the detection of Cd2+ through square wave voltammetry. Effect of different experimental parameters was studied which include electrode preparation, frequency, and amplitude. The electrochemical characterization of the electrode was done using the cyclic voltammetry and electrochemical impedance spectroscopy (EIS), the modified electrode was found conductive with much improved electrochemical performances. The obtained detection limit for Cd2+ sensing was 9.39 ppb, the developed C-dots modified GCE electrode was also tested with tap water Cd2+ spiked solution to demonstrate its implementation in real sample analysis. , Thesis (MA) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
Keratinous poultry waste valorization through novel keratinases of C. cucumeris and S. multivorium isolated from poultry sludge
- Authors: Qaphela, Hendrick
- Date: 2021-02
- Subjects: Food--Biotechnology , Poultry , Poultry industry
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20860 , vital:46640
- Description: Annually, about 55 percent of keratinous wastes are generated from various agro-industrial processing farms in South Africa. These wastes are difficult to handle due to structural integrity; hence, they constitute environmental issues due to the disposal means. Degradation of keratinous wastes using microbial-based technology has been deemed advantageous as it generates products with high-end values. Therefore, in this study, chicken feather and soil samples were collected from a local poultry farm, and bacteria were isolated using basal salt media supplemented with chicken feathers. The isolates were evaluated for proteolytic and keratinolytic potentials. The potent isolates were identified through 16S rDNA sequence and phylogenetic analysis. Fermentation media were optimized for enhanced keratinase production, and the amino acids liberated in the media during feather biodegradation were quantified. The biochemical properties of the keratinases produced were likewise determined. Ten (10) proteolytic bacteria were obtained from 20 isolates recovered from the samples with a diameter of halo on skimmed milk agar plate ranging from 15.5 ± 0.71 (mm) for isolate coded as PSW-15 to 28 ± 1.41 (mm) for isolate coded as PSW-08. The proteolytic bacteria showed variable keratinolytic potentials with percentage feather degradation that ranged from 29 percent for PSW-11 to 84 percent for PSW-14, and keratinase activity ranging from 99.99 U/mL for PSW-15 to 761.82 U/mL for PSW-14. The most potent isolates coded as PSW-14 and PSW-16 were identified as Chryseobacterium cucumeris FHN1 and Sphingobacterium multivorum HNFx. Their nucleotide sequences were submitted to the GenBank as MW16587 and MK82939, respectively. The optimization of fermentation conditions; C. cucumeris FHN1 showed improved activity at pH 5 - 6, inoculum size (4 percent, v/v), chicken feather concentration (1 percent, w/v), fermentation temperature (25o C). Similarly, S. multivorum HNFx showed optimal activity at pH 4.0, inoculum size (5 percent, v/v), chicken feather concentration (2.5 percent, w/v), and fermentation temperature (25-30 oC). C. cucumeris FHN1 and S. multivorum HNFx showed maximum keratinase production of 485.54 U/mL and 526.36 U/mL at 96 h and 72 h of incubation period respectively. Serine, aspartic acid, glutamic acid, and proline were the most abundant amino acids in the degraded chicken feathers, and upon quantitation, the following concentration was respectively obtained; 3.71, 3.4, 4.19 and 4.35 (g/100g sample) against C. cucumeris FHN1. While S. multivorum HNFx yielded aspartic acid (2.04 g/100g sample) and glutamic acid (2.0 g/100g sample) in high concentration. The keratinases showed optimal catalytic efficiency at pH and temperature of 8.0 and 90 oC, respectively. C. cucumeris FHN1 keratinase was inhibited by metal ion chelating agents; EDTA and 1,10-phenanthroline, suggesting a metallo-type of protease. The enzyme showed remarkable stability after pre-treatment with DTT, Fe2+, Fe3+ and Cu2+, with respective residual activity of 108 percent, 102 percent, 114 percent, and 104 percent. The S. multivorum HNFx keratinase; activity was not inhibited by serine- and metallo-protease inhibitors. It maintained the following residual activity against the following chemical agents; DTT (124 percent), hydrogen peroxide (152 percent), DMSO (161 percent), triton X-100 (152 percent), tween-80 (101 percent), and metal ions; Fe2+ (128 percent), Fe3+ (104 percent), K+ (117 percent), Ca2+ (104 percent), Na+ (103 percent), Ba2+ (115 percent), Al3+ (126 percent). The enzyme showed a substantial loss of catalytic efficiency after pre-incubation with various laundry detergents. The keratinases' remarkable stability in the presence of various chemical agents and metal ions tested suggests biotechnological and industrial application potentials. Consequently, the isolates portend industrial relevance for keratinous waste valorization and an excellent source of keratinases of industrial relevance. , Thesis (MSc) (Microbiology) -- University of Fort Hare, 2021
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- Date Issued: 2021-02
Keratinous poultry wastes valorization through novel keratinases of Chryseobacterium cucumeris and Sphingobacterium multivorum isolated from poultry sludge
- Authors: Hendrick, Qaphela https://orcid.org/0000-0001-7529-8129
- Date: 2021-02
- Subjects: Agricultural wastes , Factory and trade waste
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/21400 , vital:48537
- Description: Annually, about 55percent of keratinous wastes are generated from various agro-industrial processing farms in South Africa. These wastes are difficult to handle due to structural integrity; hence, they constitute environmental issues due to the disposal means. Degradation of keratinous wastes using microbial-based technology has been deemed advantageous as it generates products with high-end values. Therefore, in this study, chicken feather and soil samples were collected from a local poultry farm, and bacteria were isolated using basal salt media supplemented with chicken feathers. The isolates were evaluated for proteolytic and keratinolytic potentials. The potent isolates were identified through 16S rDNA sequence and phylogenetic analysis. Fermentation media were optimized for enhanced keratinase production, and the amino acids liberated in the media during feather biodegradation were quantified. The biochemical properties of the keratinases produced were likewise determined. Ten (10) proteolytic bacteria were obtained from 20 isolates recovered from the samples with a diameter of halo on skimmed milk agar plate ranging from 15.5 ± 0.71 (mm) for isolate coded as PSW-15 to 28 ± 1.41 (mm) for isolate coded as PSW-08. The proteolytic bacteria showed variable keratinolytic potentials with percentage feather degradation that ranged from 29percent for PSW-11 to 84percent for PSW-14, and keratinase activity ranging from 99.99 U/mL for PSW-15 to 761.82 U/mL for PSW-14. The most potent isolates coded as PSW-14 and PSW-16 were identified as Chryseobacterium cucumeris FHN1 and Sphingobacterium multivorum HNFx. Their nucleotide sequences were submitted to the GenBank as MW16587 and MK82939, respectively. The optimization of fermentation conditions; C. cucumeris FHN1 showed improved activity at pH 5 - 6, inoculum size (4percent, v/v), chicken feather concentration (1percent, w/v), fermentation temperature (25o C). Similarly, S. multivorum HNFx showed optimal activity at pH 4.0, inoculum size (5percent, v/v), chicken feather concentration (2.5percent, w/v), and fermentation temperature (25-30 oC). C. cucumeris FHN1 and S. multivorum HNFx showed maximum keratinase production of 485.54 U/mL and 526.36 U/mL at 96 h and 72 h of incubation period respectively. Serine, aspartic acid, glutamic acid, and proline were the most abundant amino acids in the degraded chicken feathers, and upon quantitation, the following concentration was respectively obtained; 3.71, 3.4, 4.19 and 4.35 (g/100g sample) against C. cucumeris FHN1. While S. multivorum HNFx yielded aspartic acid (2.04 g/100g sample) and glutamic acid (2.0 g/100g sample) in high concentration. The keratinases showed optimal catalytic efficiency at pH and temperature of 8.0 and 90 oC, respectively. C. cucumeris FHN1 keratinase was inhibited by metal ion chelating agents; EDTA and 1,10-phenanthroline, suggesting a metallo-type of protease. The enzyme showed remarkable stability after pre-treatment with DTT, Fe2+, Fe3+ and Cu2+, with respective residual activity of 108percent, 102percent, 114percent, and 104percent. The S. multivorum HNFx keratinase; activity was not inhibited by serine- and metallo-protease inhibitors. It maintained the following residual activity against the following chemical agents; DTT (124percent), hydrogen peroxide (152percent), DMSO (161percent), triton X-100 (152percent), tween-80 (101percent), and metal ions; Fe2+ (128percent), Fe3+ (104percent), K+ (117percent), Ca2+ (104percent), Na+ (103percent), Ba2+ (115percent), Al3+ (126percent). The enzyme showed a substantial loss of catalytic efficiency after pre-incubation with various laundry detergents. The keratinases' remarkable stability in the presence of various chemical agents and metal ions tested suggests biotechnological and industrial application potentials. Consequently, the isolates portend industrial relevance for keratinous waste valorization and an excellent source of keratinases of industrial relevance. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
The acoustic niche and conservation status of the recently described Hogsback caco, Cacosternum thorini (Amphibia: Pyxicephalidae), Hogsback, Eastern Cape, South Africa
- Authors: Kom, Nokuthula
- Date: 2021-02
- Subjects: Amphibians
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20429 , vital:45665
- Description: Animals may compete for acoustic space (acoustic niche) in the same way they do for habitat space. The most intense competition involves individuals with the most similar resource requirements (i.e. conspecifics), but if competition is interspecific, then mate recognition must occur both within and between species. The coexistence of the bronze caco (Cacosternum nanum) and the Hogsback caco (C. thorini) in the Tor Doone area of Hogsback could be interpreted as a result of past competition, which drove acoustic partitioning by means of the evolution of specific calls that do not overlap in frequency. Frogs are known to coexist well with other frog species because of their highly specific advertisement calls, which differ even between closely related species. One of the main aims of the project was to record and provide a description of the call of the recently described Hogsback caco, C. thorini. I identified 30 calling males and recorded each for 10 min in February 2016, yielding a total of 235 calls. Summary values for the calls include duration of 40 ± 14 ms, with 16 ± 5 pulses produced at a pulse-rate of 46 ± 21 s-1 and a mean dominant frequency of 4.19 ± 0.58 kHz. The call of C. thorini differs from those of all other cacos, by its incremental structure (increased number of pulses within consecutive units). My second goal was to use playbacks to investigate the preferred habitat of C. thorini and to compare it with that of C. nanum. I conducted experiments to measure the propagation of C. thorini and C. nanum calls in three different habitats (C. thorini habitat, C. nanum habitat, and grassland with no water bodies). Finally, I investigated the effect of drought and flood on the pools used by males as calling sites, using a buried basin to which I added water in 10 litre aliquots. The optimal water level for call propagation in the artificial pools was half-full. Using playbacks, I tested whether the two species responded to each other’s calls. I found that, although the two species call at the same time and each call in response to the other’s calls, they do not recognise heterospecific calls; they simply respond to noise. I found no evidence of acoustic competition between the two species, and in fact, the abundant, dominant species, C. nanum, was rare in the C. thorini preferred habitat. The results of this study may assist efforts to conserve endemic amphibians in the Amatola Mountains. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
The Relationship Between Food Sharing and Social Cohesion among Local Farmers: a case study of Ntafufu Location, Port St Johns Municipality.
- Authors: Mphompo, Aphiwe (https://orcid.org/ 0000-0003-0370-8007)
- Date: 2021-02
- Subjects: Food supply , Social integration , Food relief
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20981 , vital:46876
- Description: The overall aim of this study was to examine how food sharing at Ntafufu location in Port St Johns (Republic of South Africa), augments social cohesion among local farmers. A mixed-method approach was used for this study. This study used a triangulation research method to measure the correlation between food sharing and social cohesion and to ensure that it is statistically sound, certainly gaining rich data from the study population. Focus groups and questionnaires were used to collect data. The researcher used thematic analysis for qualitative analysis and Statistical Packages for the Social Science (SPSS) for quantitative analysis. The researcher did not include the whole population. The researcher only interviewed selected participants, and these participants were taken from the study population. There were 13 participants for qualitative research and 43 participants for quantitative research totalling 56 participants. The findings revealed that there is a relationship between food sharing and social cohesion. An important finding to emerge in this study is that food sharing alleviates poverty. However, several limitations need to be considered. For instance, witchcraft was mentioned as a challenge for this practice. , Thesis (MSoc) (Anthropology) -- University of Fort Hare, 2021
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- Date Issued: 2021-02
Valorization of chicken feather through dekeratinization by keratinolytic Bacillus species to amino acid
- Authors: Matches, Lupho
- Date: 2021-02
- Subjects: Proteolytic enzymes , Poultry -- Processing
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20451 , vital:45667
- Description: The poultry meat processing sector generates chicken feathers as by-products, and they are 90percent keratin in composition. Keratin is an insoluble and structural protein that shows recalcitrance to hydrolysis by classical proteolytic enzymes, including trypsin, pepsin, and papain. Keratinases are a group of proteolytic enzymes endowed with keratin degradation into peptides and amino acids. They are recently gaining traction for their multifaceted potential application in the green industrial space. Hence, keratinolytic bacteria previously isolated from dumpsite were identified using 16S rDNA sequencing. The optimal fermentation conditions were determined for enhanced extracellular keratinase production and chicken feather degradation. Also, the amino acid analysis of the chicken feather hydrolysates was carried out. The biochemical properties of the keratinases were also determined. Based on 16S rDNA sequencing and phylogenetic analysis, the isolates coded as SSN-02 and HSN-03 showed a high percentage of sequence homology with Bacillus spp.; hence, they were identified as Bacillus sp. NFH5 and Bacillus sp. FHNM, respectively. Bacillus sp. NFH5 showed optimal keratinase production of 1149.99 ± 80.99 U/mL after 96 h of incubation time, in optimized fermentation conditions that included pH (4.0), chicken feather (1.5percent, w/v), inoculum size (3percent, v/v) and temperature (30 oC). Similarly, Bacillus sp. FHNM demonstrated the maximum keratinase production of 480 ± 41.14 U/mL 144 h post cultivation, in optimized fermentation conditions with pH (7.0), chicken feather (2.0percent, w/v), inoculum size (3percent, v/v) and temperature (30 oC). For Bacillus sp. NFH5 chicken feather hydrolysate, the amino acids in relatively higher concentration (>1.0g/100g sample) include arginine (1.8), serine (1.16), aspartic acid (1.95), glutamic acid (2.47), proline (1.16) and glycine (1.45). Bacillus sp. FHNM feather hydrolysates, contained (g/100g of sample): arginine (1.9), serine (1.4), aspartic acid (2.5), glutamic acid (2.51), glycine (1.51), proline (1.13), leucine (1.030, histidine (1.25), and lysine (1.06) (g/100g of sample) in high concentration. The keratinases were optimally active at pH 8.0. Bacillus sp. FHNM showed an optimal temperature of 100 oC; while Bacillus sp. NFH5 keratinase displayed optimal activity at 90 oC. EDTA and 1,10-phenanthroline inhibited the keratinases, and the inhibition pattern indicated that they belong to metalloprotease. Keratinase from Bacillus sp. FHNM showed considerable residual activity in the presence of Co²⁺ (93percent), Fe³⁺ (99percent), and K⁺ (94percent). Bacillus sp. NFH5 keratinase retained 92percent, 92percent, 93percent of the original activity against Ba²⁺, Na⁺ and Fe³⁺ treatment. Bacillus sp. FHNM keratinase was remarkably stable after 60 min of detergents treatment with residual activity of 89percent, 96percent, 81percent, 73percent, 96percent, 88percent, 88percent and 98percent for Omo, Surf, Ariel, Sunlight, Prowash, Freshwave, Sky, and Evaklin, respectively. Maq impacted the enzyme stability negatively, with residual activity of 48percent after 60 min of incubation. Additionally, keratinase Bacillus sp. NFH5 retained 68percent, 78percent, 80percent, 84percent, 57percent, 80percent, 98percent, 106percent and 106percent of the original activity against Omo, Surf, Ariel, Sunlight, Maq, Prowash, Freshwave, Sky and Evaklin, respectively. Therefore, these results suggest that Bacillus spp. could be ideal candidates for sustainable production of active keratinases and valorization of the abundantly generated keratinous biomass. The stability displayed by keratinases from Bacillus sp. FHNM and Bacillus sp. NFH5 suggests their promising candidacy for detergent formulation. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02
Waste keratinous biomass valorization and characterization of keratinases produced by exiguobacteria species
- Authors: Dlume, Tutuka
- Date: 2021-02
- Subjects: Factory and trade waste -- Biodegradation , Bioremediation
- Language: English
- Type: Master's theses , text
- Identifier: http://hdl.handle.net/10353/20695 , vital:46438
- Description: Keratinous wastes are emanating in a million tons, as by-products, from various agro-industrial processing plants. Consequently, they create a serious solid waste problem in the environment due to poor handling. Microbial keratinases are proteolytic enzymes that effectively participate in keratin-rich biomass hydrolyses such as feathers, nail, hair, hooves, and horns. Therefore, proper management of these wastes via recycling into useful products is ecologically imperative. Biodegradation of keratin-rich biomass has been identified as an economical and environmentally friendly way of transforming these recalcitrant agro wastes into useful products, hence the motivation for this study. Feather degrading bacterial strains previously isolated from a municipal dumpsite and coded as SSB-02 and SSB-03 was identified through 16S rDNA sequencing and phylogenetic analysis. The fermentation conditions for keratinase production were optimized. The protein and amino acids constituents of the hydrolyzed chicken feather were analyzed. The biochemical properties of the keratinase produced were determined. Also, the effect of laundry detergents on the stability of the keratinase was studied. The isolates coded as SSB-02 and SSB-03 showed a high percentage of sequence homology with Exguobacterium spp., hence they were identified as Exiguobacterium sp. FBH5 and Exiguobacterium acetylicum FHBD, respectively. Exiguobacterium sp. FBH5 showed the highest extracellular keratinase production of 934.58 ± 27.27 U/mL at 72 h of incubation; in optimized fermentation conditions that included pH (5.0), temperature (30 oC), and chicken feather (0.5percent, w/v). Similarly, E. acetylicum FHBD displayed optimal keratinase production of 1023.64 ± 25.71 U/mL at 120 h of fermentation and improved fermentation conditions that involved pH (3.0), temperature (35 oC) and chicken feathers (0.5-1.5percent; w/v). The amino acid analysis showed that arginine, aspartic acid and glutamic acid were the most abundant amino acids cleaved from the degradation of chicken feathers by Exiguobacterium sp. FBH5 at a respective concentration of 1.16, 1.28 and 1.45 (g/100g sample). Additionally, hydrolysate that emanated from E. indicum FHBD degradation of feather showed high concentrations of arginine, serine, aspartic acid, glutamic acid, and glycine at the respective concentration (g/100g sample) of 1.2, 1.12, 1.34, 1.58 and 1.29. The keratinases were optimally active at pH and temperature of 8.0 and 50 oC, respectively. EDTA and PMSF did not highly repress keratinolytic proteases' activity, and this inhibitory pattern suggests that they may belong to a mixed protease family. Keratinase from E. acetylicum FHBD was highly stable in the presence of SDS, with 99percent residual activity and displayed variable stability in other chemical agents tested. A similar stability pattern was observed with keratinase from Exiguobacterium sp. FBH5, although the enzyme lost about 40percent of its original activity in the presence of SDS. Evaluation of metal ion stability indicated that E. acetylicum FHBD keratinase was remarkably stable in the presence of Fe3+, Mg2+, Cu2+, Zn2+, and Ba2+, with residual activity of 94percent, 88percent, 89percent, 90percent, and 97percent, respectively. Similarly, Exiguobacterium sp. FBH5 keratinase was considerably stable after treatment with Co2+, K+, and Zn2+ as it displayed a residual activity of 85percent, 84percent and 93percent, respectively. The study of the keratinases stability in laundry detergents showed that E. acetylicum FHBD keratinolytic proteases was activated in the presence of Omo, Surf, Sunlight, and Pro wash after 60 min of pre-incubation compared to 30 min, with residual activity of 94 ± 2.94percent, 91 ± 2.53percent, 95 ± 2.89percent and 87 ± 2.89percent respectively. Likewise, Exiguobacterium sp. FBH5 keratinase activity was promoted after 60 min of incubation compared to 30 min, with a residual enzyme activity of 79percent, 84percent, 101percent, 103percent and 105percent and 106percent for Ariel, Surf, Prowash, Freewave, Sky and Evaklin, respectively. Therefore Exiguobacterium spp., demonstrated excellent keratinolytic potentials that could be exploited for sustainable development of bio-innovative products. The study keratinases' properties suggest their industrial and biotechnological application potentials, especially as bio-additive in the formulation of laundry detergents. , Thesis (MSc) -- Faculty of Science and Agriculture, 2021
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- Date Issued: 2021-02