Characterization of arginase from the liver of mango tilapia (sarotherodongalilaeus)
Table Of Contents
- HAPTER ONE: INTRODUCTION AND LITERATURE REVIEW1.o Introduction1.2 Classification1.3 Distribution and occurrence1.4 Literature review1.
- 4.1 Arginase1.
- 4.2 Arginase isoenzymes1.5 Structural properties1.
- 5.1 Molecular properties1.
- 5.2 Amino acid composition1.6 Physicochemical properties1.
- 6.1 Kinetic properties1.
- 6.2 Effect of p H1.
- 6.3 Effect of temperature1.
- 6.4 Effect of metal ions1.7 Mechanism of action1.8 Arginase deficiency1.9 Biological and physiological importance of arginase1.10 Study sample1.
- 10.1Taxonomy1.
- 10.2Morphology1.
- 10.3Distribution1.
- 10.4Ecology1.
- 10.5Biology1.
- 10.6Feeding habits1.
- 10.7Reproduction and parental care1.
- 10.8Economic importance1.11 Liver1.12 ObjectivesCHAPTER TWO: MATERIALS AND METHODS2.1 Materials2.
- 1.1 Chemicals and reagents2.
- 1.2 Equipments2.2 Methods2.
- 2.1 Enzyme isolation2.
- 2.2 Preparation of buffer and reagents2.2.
- 2.10.33M Arginine2.2.
- 2.2Bradford reagent2.2.
- 2.3Erlich reagent2.2.
- 2.4Homogenization buffer (0.1M Phosphate buffer)2.2.
- 2.50.1M Citrate buffer, p H 3.02.2.
- 2.60.1M Trizma HCl buffer, p H 6.02.2.
- 2.70.1M Trizma HCl buffer, p H 7.02.2.
- 2.80.1M Trizma HCl buffer, p H 9.02.2.
- 2.9Arginase assay2.2.
- 2.10Protein assay2.2.
- 2.11Determination of kinetic parameters2.2.
- 2.12Effect of p H on enzyme activity2.2.
- 2.13Effect of temperature on enzyme activity2.2.
- 2.14Effect of amino acids on enzyme activity2.2.
- 2.15Effect of chelating compounds on arginase activity2.2.
- 2.16Effect of metal ions on arginase activityCHAPTER THREE: RESULTS3.1 Effect of temperature3.2 Effect of pH3.3 Kinetic study3.4 Inhibition study3.
- 4.1Effect of chelating compounds3.
- 4.2Effect of divalent metals3.
- 4.3Effect of amino acidsCHAPTER FOUR: DISCUSSION, CONCLUSION AND RECOMMENDATION4.1 Discussion4.2 Conclusion4.3 RecommendationReferencesLIST OF TABLESTable
- 3.1 Effect of temperature on arginase activityTable
- 3.2 Effect of pH on arginase activityTable
- 3.3 Kinetic studyTable
- 3.4 Effect of chelating compoundsTable
- 3.5 Effect of divalent metalsTable
- 3.6 Effect of amino acidsLIST OF FIGURESFigure
- 1.1 External structure of mango tilapiaFigure
- 3.1 Graph of temperature against activityFigure
- 3.2 Graph of pH against activityFigure
- 3.3 Determination of Km and Vmax
Thesis Abstract
Arginase is a detoxifying enzyme that catalyses the hydrolysis of arginine into ornithine and urea, the last step of urea cycle- a process through which the body disposes off harmful ammonia. This research was carried out to determine the characteristics of liver arginase of mango tilapia (Sarotherodongalilaeus) in Opa river, Osun state.
The enzyme ‘arginase’ was isolated from the liver of mango tilapia through the process of homogenization and centrifugation which was done at 4000rev/min.The protein concentration was determined using Bradford method and the arginase assay was determined by Kaysen and Strecker method.
The kinetic study shows that mango tilapia of liver arginase has a Km value of 0.2M and a Vmax value of 166.7µmol/ml/min. The effect of temperature on arginase activity was tested and the optimum temperature for mango tilapia liver arginase is 50°C at activity of 63.44µmol/ml/min. The effect of pH was also investigated and optimum pH is 8.0 at activity of 165.1µmol/ml/min. Inhibition study was also carried out and it was observed that calcium (51.4±1.13) and zinc (51.5±4.27) strongly inhibit arginase while mercury, magnesium and sodium have little or no inhibitory effect on arginase. Also from the result, it can be deduce that citrate (20.8±4.67) and glutathione (28.6±2.53) and ethylenediamineacetic acid (EDTA) slightly inhibit arginase while urea has les inhibitory effect on arginase. The result for the effect of amino acids on enzyme activity shows that liver arginase of mango tilapia to be in this order arginine > valine> aspartate > cysteine > lysine with residual activity of 107.2%, 86.6%, 73.4%, 62.1% and 58.7% respectively.
Mango tilapia liver arginase belongs to the ureotelic class of arginases according to Mora J et al classification (1965). It has a Km value of 0.2M and aVmax value of 166.7µmol/ml/min.
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