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Sparklyn Characterization of Arginase from the Liver of Mango Tilapia (Sarotherodongalilaeus)
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Characterization of Arginase from the Liver of Mango Tilapia (Sarotherodongalilaeus)

This page presents an excerpt of the research material, providing a comprehensive overview of the study. It includes the Preliminary Pages, Table of Contents, Abstract, Chapters One to Five, and References, making it accessible and informative for students, researchers, and other readers interested in the topic of this study. Acknowledgement is also included, expressing gratitude to the individuals, institutions, and resources that contributed to the successful completion of the research, with materials and information sourced from the online platform sparklyn.com.ng, which provided valuable academic support.

TABLE OF CONTENTS

PRELIMINARY PAGES

  • Title page
  • Approval page
  • Dedication
  • Acknowledgement
  • Table of Contents
  • Abstract

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.

CHAPTER ONE

1.1 Introduction

In this section, Characterization of Arginase from the Liver of Mango Tilapia (Sarotherodongalilaeus) is discussed, with relevant and recent citations. 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 terms.

CHAPTER TWO

LITERATURE REVIEW

2.1 Introduction

This chapter focuses on the review of related literature. A literature review presents current knowledge, as well as theoretical and methodological contributions, related to Characterization of Arginase from the Liver of Mango Tilapia (Sarotherodongalilaeus). It documents the state of the art on the subject under study and provides a comprehensive survey of existing literature. In this research work the literature review includes the conceputal review, theoretical framework, the review of related literature …

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