Studies on the activity of ∞-amylase produced from fusarium spp. using sweet potato (ipomoea batatas) starch.

 

Table Of Contents


Chapter ONE

INTRODUCTION

  • 1.1Introduction
  • 1.2Background of Study
  • 1.3Problem Statement
  • 1.4Objective of Study
  • 1.5Limitation of Study
  • 1.6Scope of Study
  • 1.7Significance of Study
  • 1.8Structure of the Research
  • 1.9Definition of Terms

Chapter TWO

LITERATURE REVIEW

  • 2.1Overview of ∞-Amylase
  • 2.2Production of ∞-Amylase from Fusarium spp.
  • 2.3Properties of ∞-Amylase
  • 2.4Role of Sweet Potato Starch in ∞-Amylase Production
  • 2.5Enzyme Kinetics of ∞-Amylase
  • 2.6Applications of ∞-Amylase
  • 2.7Factors Affecting ∞-Amylase Activity
  • 2.8Comparison of ∞-Amylase from Different Sources
  • 2.9Industrial Uses of ∞-Amylase
  • 2.10Recent Advances in ∞-Amylase Research

Chapter THREE

RESEARCH METHODOLOGY

  • 3.1Research Design
  • 3.2Sampling Techniques
  • 3.3Data Collection Methods
  • 3.4Experimental Setup
  • 3.5Variables and Measurements
  • 3.6Data Analysis Techniques
  • 3.7Ethical Considerations
  • 3.8Research Limitations

Chapter FOUR

DATA PRESENTATION AND ANALYSIS

  • 4.1Overview of Findings
  • 4.2Analysis of Data
  • 4.3Comparison of Results
  • 4.4Interpretation of Results
  • 4.5Discussion on ∞-Amylase Activity
  • 4.6Impact of Sweet Potato Starch
  • 4.7Implications for Future Research
  • 4.8Recommendations

Chapter FIVE

SUMMARY, CONCLUSION AND RECOMMENDATIONS

  • 5.1Summary of Findings
  • 5.2Conclusion
  • 5.3Contributions to Knowledge
  • 5.4Practical Implications
  • 5.5Recommendations for Further Research

Project Abstract

<p> After a seven day pilot studies, day 6 was found suitable for enzyme production from Fusarium species using starch from Ipomoea batatas (sweet potato) tubers as the carbon source. The specific activity of the crude enzyme was 55.45µ/mg. After ammonium sulphate precipitation and gel filtration, the specific activities were found to be 35.93µ/mg and 119.61µ/mg, respectively which corresponds to 3.33 fold purification. The optimum pH and temperature of the partially purified enzyme were 6.0 and 50oC, respectively. The enzyme activity was strongly activated by Mn2+, Ca2+, and Mg2+ but inhibited by Co2+. The Michaeligs constant (Km) and maximum velocity (Vmax) obtained from the Lineweaver-Burk plot of initial velocity data at different substrate concentrations were 5.44mg/ml and 12.57µmol/min, respectively. <br></p>

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