Financial reforms and interest rate spreads in the commercial banking sector in Kenya
- Authors: Munene, Daniel
- Date: 2006
- Subjects: Finance -- Kenya , Banks and banking -- Kenya , Economics -- Kenya , Interest rates -- Kenya , Economic development -- Kenya
- Language: English
- Type: Thesis , Masters , MCom
- Identifier: vital:1070 , http://hdl.handle.net/10962/d1007711 , Finance -- Kenya , Banks and banking -- Kenya , Economics -- Kenya , Interest rates -- Kenya , Economic development -- Kenya
- Description: Financial reforms were a major component of structural adjustment programs deemed necessary for developing countries in the mid 1980s. These were not only meant to improve the sector, but would ultimately enhance economic growth and help in poverty alleviation. At the top of these reforms was financial liberalisation. Kenya, like many other sub-Saharan African countries, undertook financial liberalisation in 1991, one of the measures was decontrolling interest rates. With market driven interest rates in place it was assumed that there would be increased efficiency in bank lending, as well as growth in credit availability as deposits increased. A key indicator of this improved intermediation process would be a narrowing interest rates spread, that is, the margin between the deposit and lending rate. Paradoxically, however, the expected benefits of these reforms did not accrue to Kenya's banking sector. This study focuses on financial reforms and the spread of interest rates in Kenya's banking sector. Using a trend analysis, spanning the period before and after liberalisation, interest rates spread are shown to have escalated dramatically upwards after liberalisation. An analysis of three macroeconomic variables, namely, the exchange rate, inflation rate and economic growth offer little, or inconclusive evidence, that they were the main causes of the wide interest rate spread. In fact, the spread is closely linked to institutional/structural factors such as non-competitiveness in the banking sector, imprudent lending practices and poor and/or inadequate banking supervision. Policies for improving the institutional infrastructure and thus moderating the spreads are highlighted.
- Full Text:
- Authors: Munene, Daniel
- Date: 2006
- Subjects: Finance -- Kenya , Banks and banking -- Kenya , Economics -- Kenya , Interest rates -- Kenya , Economic development -- Kenya
- Language: English
- Type: Thesis , Masters , MCom
- Identifier: vital:1070 , http://hdl.handle.net/10962/d1007711 , Finance -- Kenya , Banks and banking -- Kenya , Economics -- Kenya , Interest rates -- Kenya , Economic development -- Kenya
- Description: Financial reforms were a major component of structural adjustment programs deemed necessary for developing countries in the mid 1980s. These were not only meant to improve the sector, but would ultimately enhance economic growth and help in poverty alleviation. At the top of these reforms was financial liberalisation. Kenya, like many other sub-Saharan African countries, undertook financial liberalisation in 1991, one of the measures was decontrolling interest rates. With market driven interest rates in place it was assumed that there would be increased efficiency in bank lending, as well as growth in credit availability as deposits increased. A key indicator of this improved intermediation process would be a narrowing interest rates spread, that is, the margin between the deposit and lending rate. Paradoxically, however, the expected benefits of these reforms did not accrue to Kenya's banking sector. This study focuses on financial reforms and the spread of interest rates in Kenya's banking sector. Using a trend analysis, spanning the period before and after liberalisation, interest rates spread are shown to have escalated dramatically upwards after liberalisation. An analysis of three macroeconomic variables, namely, the exchange rate, inflation rate and economic growth offer little, or inconclusive evidence, that they were the main causes of the wide interest rate spread. In fact, the spread is closely linked to institutional/structural factors such as non-competitiveness in the banking sector, imprudent lending practices and poor and/or inadequate banking supervision. Policies for improving the institutional infrastructure and thus moderating the spreads are highlighted.
- Full Text:
Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42
- Authors: Simpson, Clinton
- Date: 2006
- Subjects: Penicillium , Glucose , Oxidases
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3975 , http://hdl.handle.net/10962/d1004034 , Penicillium , Glucose , Oxidases
- Description: A novel glucose oxidase from Penicillium canescens (Tt42) was isolated, purified and characterised. The P. canescens Tt42 was cultivated using an optimised growth medium from literature, and maximum glucose oxidase activities of 11.5 U/ml and 6.9 U/ml for the intra- and extracellular fractions were obtained. Maximum glucose oxidase production was achieved after 72 hours at 28°C which coincided with glucose depletion. A total of 1104 U (from 60ml) of glucose oxidase was produced with a biomass specific glucose oxidase activity of 1.08 Umg[superscript -1] Four methods of cell disruption were evaluated for release of intracellular glucose oxidase from P. canescens Tt42 cells. These methods were; sonication, French press, Freeze-Thaw and a high pressure cell disrupter (Z-Plus Series) from Constant systems. All the methods were successful in releasing the intracellular glucose oxidase from P. canescens Tt42. The use of the Constant Systems high pressure cell disrupter was preferred, since it was the simplest and most rapid method. Ammonium sulphate precipitation was shown to be effective as an initial purification step for extracellular glucose oxidase from P. canescens Tt42. Comparison of the intra- and extracellular glucose oxidase fractions using isoelectric focusing showed 2 isoenzymes in both fractions. The pI values of the isoenzymes were determined to be 4.30 and 4.67, with the former being dominant. Since both the intra- and extracellular fractions contained the same isoenzymes of glucose oxidase, further purification studies were performed using the extracellular fraction. The glucose oxidase from P. canescens Tt42 was purified using 3 main techniques: ammonium sulphate precipitation (60% - 70% cut), anion exchange chromatography (Super Q 650M) and size exclusion chromatography (Sephadex S200HR). The glucose oxidase was determined to be ±80% pure by size exclusion chromatography. The final purified glucose oxidase was lyophilised, and an overall purification yield of 10.3% was achieved with an 8.6-fold purification. The purified glucose oxidase was confirmed to be catalase free. Glucose oxidase from P. canescens Tt42 was determined to be a dimeric protein (M[subscript r] ±148kDa) likely consisting of 2 equal subunits (M[subscript r] ± 70kDa). The temperature optimum range was shown to be 25-30°C. The optimum pH for the oxidation of β-D-glucose was pH 7. The enzyme was shown to be stable at 25°C for 10 hours, with a half life of approximately 30 minutes at 37°C. The lyophilised enzyme was stable at -20°C for 6 months. The properties of glucose oxidase from Tt42 were comparable to alternative glucose oxidase enzymes from Aspergillus and other Penicillium species. Glucose oxidase from P. canescens Tt42 was shown to have distinct kinetic characteristics. The V[subscript max] and K[subscript m] were shown to be 651 Umg[superscript -1] and 18.4 mM towards β-D-glucose. The catalytic kcat and specificity k[subscript cat]/K[subscript m] constants for glucose oxidase from P. canescens Tt42 were shown to be 791 s[superscript -1] and 40 s[superscript -1]mM[superscript -1] each respectively. The specificity constant (k[subscript cat]/K[subscript m]) of glucose oxidase from P. canescens Tt42 was determined to be 1.3-fold higher than that that of A. niger (Sigma Type VII) and 8.7-fold lower than that of P. amagasakiense (ATCC 28686) from literature.
- Full Text:
- Authors: Simpson, Clinton
- Date: 2006
- Subjects: Penicillium , Glucose , Oxidases
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3975 , http://hdl.handle.net/10962/d1004034 , Penicillium , Glucose , Oxidases
- Description: A novel glucose oxidase from Penicillium canescens (Tt42) was isolated, purified and characterised. The P. canescens Tt42 was cultivated using an optimised growth medium from literature, and maximum glucose oxidase activities of 11.5 U/ml and 6.9 U/ml for the intra- and extracellular fractions were obtained. Maximum glucose oxidase production was achieved after 72 hours at 28°C which coincided with glucose depletion. A total of 1104 U (from 60ml) of glucose oxidase was produced with a biomass specific glucose oxidase activity of 1.08 Umg[superscript -1] Four methods of cell disruption were evaluated for release of intracellular glucose oxidase from P. canescens Tt42 cells. These methods were; sonication, French press, Freeze-Thaw and a high pressure cell disrupter (Z-Plus Series) from Constant systems. All the methods were successful in releasing the intracellular glucose oxidase from P. canescens Tt42. The use of the Constant Systems high pressure cell disrupter was preferred, since it was the simplest and most rapid method. Ammonium sulphate precipitation was shown to be effective as an initial purification step for extracellular glucose oxidase from P. canescens Tt42. Comparison of the intra- and extracellular glucose oxidase fractions using isoelectric focusing showed 2 isoenzymes in both fractions. The pI values of the isoenzymes were determined to be 4.30 and 4.67, with the former being dominant. Since both the intra- and extracellular fractions contained the same isoenzymes of glucose oxidase, further purification studies were performed using the extracellular fraction. The glucose oxidase from P. canescens Tt42 was purified using 3 main techniques: ammonium sulphate precipitation (60% - 70% cut), anion exchange chromatography (Super Q 650M) and size exclusion chromatography (Sephadex S200HR). The glucose oxidase was determined to be ±80% pure by size exclusion chromatography. The final purified glucose oxidase was lyophilised, and an overall purification yield of 10.3% was achieved with an 8.6-fold purification. The purified glucose oxidase was confirmed to be catalase free. Glucose oxidase from P. canescens Tt42 was determined to be a dimeric protein (M[subscript r] ±148kDa) likely consisting of 2 equal subunits (M[subscript r] ± 70kDa). The temperature optimum range was shown to be 25-30°C. The optimum pH for the oxidation of β-D-glucose was pH 7. The enzyme was shown to be stable at 25°C for 10 hours, with a half life of approximately 30 minutes at 37°C. The lyophilised enzyme was stable at -20°C for 6 months. The properties of glucose oxidase from Tt42 were comparable to alternative glucose oxidase enzymes from Aspergillus and other Penicillium species. Glucose oxidase from P. canescens Tt42 was shown to have distinct kinetic characteristics. The V[subscript max] and K[subscript m] were shown to be 651 Umg[superscript -1] and 18.4 mM towards β-D-glucose. The catalytic kcat and specificity k[subscript cat]/K[subscript m] constants for glucose oxidase from P. canescens Tt42 were shown to be 791 s[superscript -1] and 40 s[superscript -1]mM[superscript -1] each respectively. The specificity constant (k[subscript cat]/K[subscript m]) of glucose oxidase from P. canescens Tt42 was determined to be 1.3-fold higher than that that of A. niger (Sigma Type VII) and 8.7-fold lower than that of P. amagasakiense (ATCC 28686) from literature.
- Full Text:
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