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Characterization of Arginase From the Liver of Mango Tilapia (Sarotherodongalilaeus)

Characterization of Arginase From the Liver of Mango Tilapia (Sarotherodongalilaeus)

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DEDICATION

This research material, titled “Characterization of Arginase From the Liver of Mango Tilapia (Sarotherodongalilaeus)” is dedicated to God for His boundless grace and guidance. It is also a tribute to all computer enthusiasts whose contributions made my research journey smoother and enriched my documentation process, making the experience truly fulfilling.



ACKNOWLEDGEMENT

I am profoundly grateful to everyone who contributed to the successful completion of this project. I am especially grateful to my Supervisor (Name), the Head of Department (Name), and the Lecturers in the Department of Biochemistry for their invaluable guidance and support. I also acknowledge the contributions of authors and scholars whose works on Characterization of Arginase From the Liver of Mango Tilapia (Sarotherodongalilaeus) provided essential insights. Special thanks go to my study area (and any funding organizations, if applicable) for their financial assistance. I am equally thankful to stakeholders, including mentors, teachers, and colleagues, for their encouragement and support. Finally, I deeply appreciate my family and friends for their patience and unwavering support throughout this journey. Your contributions have been instrumental in making this research a reality.



TABLE OF CONTENTS

PRELIMINARY PAGES

CHAPTER ONE:

  • Introduction And Literature Review
  • 1.o Introduction
  • 1.2 Classification
  • 1.3 Distribution and occurrence
  • 1.4 Literature review
  • 1.4.1 Arginase
  • 1.4.2 Arginase isoenzymes
  • 1.5 Structural properties
  • 1.5.1 Molecular properties
  • 1.5.2 Amino acid composition
  • 1.6 Physicochemical properties
  • 1.6.1 Kinetic properties
  • 1.6.2 Effect of p H
  • 1.6.3 Effect of temperature
  • 1.6.4 Effect of metal ions
  • 1.7 Mechanism of action
  • 1.8 Arginase deficiency
  • 1.9 Biological and physiological importance of arginase
  • 1.10 Study sample
  • 1.10.1 Taxonomy
  • 1.10.2 Morphology
  • 1.10.3 Distribution
  • 1.10.4 Ecology
  • 1.10.5 Biology
  • 1.10.6 Feeding habits
  • 1.10.7 Reproduction and parental care
  • 1.10.8 Economic importance
  • 1.11 Liver
  • 1.12 Objectives

CHAPTER TWO:

  • Materials And Methods
  • 2.1 Materials
  • 2.1.1 Chemicals and reagents
  • 2.1.2 Equipments
  • 2.2 Methods
  • 2.2.1 Enzyme isolation
  • 2.2.2 Preparation of buffer and reagents
  • 2.2.2.1 0.33M Arginine
  • 2.2.2.2 Bradford reagent
  • 2.2.2.3 Erlich reagent
  • 2.2.2.4 Homogenization buffer (0.1M Phosphate buffer)
  • 2.2.2.5 0.1M Citrate buffer, p H 3.0
  • 2.2.2.6 0.1M Trizma HCl buffer, p H 6.0
  • 2.2.2.7 0.1M Trizma HCl buffer, p H 7.0
  • 2.2.2.8 0.1M Trizma HCl buffer, p H 9.0
  • 2.2.2.9 Arginase assay
  • 2.2.2.10 Protein assay
  • 2.2.2.11 Determination of kinetic parameters
  • 2.2.2.12 Effect of p H on enzyme activity
  • 2.2.2.13 Effect of temperature on enzyme activity
  • 2.2.2.14 Effect of amino acids on enzyme activity
  • 2.2.2.15 Effect of chelating compounds on arginase activity
  • 2.2.2.16 Effect of metal ions on arginase activity

CHAPTER THREE:

  • Results
  • 3.1 Effect of temperature
  • 3.2 Effect of pH
  • 3.3 Kinetic study
  • 3.4 Inhibition study
  • 3.4.1 Effect of chelating compounds
  • 3.4.2 Effect of divalent metals
  • 3.4.3 Effect of amino acids

CHAPTER FOUR:

  • Discussion, Conclusion And Recommendation
  • 4.1 Discussion
  • 4.2 Conclusion
  • 4.3 Recommendation
  • REFERENCES

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.


Characterization of Arginase From the Liver of Mango Tilapia (Sarotherodongalilaeus)

CHAPTER ONE

1.1 Introduction

… As a prelude to other parts of this study, this chapter will discuss the background upon which this study was initiated, the statement of problems that led to this study, the Aim and Objectives of the study. Others are Significance of the study, Scope of work, Research hypothesis and questions, Limitation of the study and Definition of technical terms.…

CHAPTER TWO

2.0 Literature Review

2.1 Introduction

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