Studies on the activity of ∞-amylase produced from fusarium spp. using sweet potato (ipomoea batatas) starch. | Blazingprojects Postgraduate Thesis
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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
  • 2.2Sources of ∞-amylase
  • 2.3Properties of ∞-amylase
  • 2.4Enzyme production
  • 2.5Sweet potato (Ipomoea batatas) starch
  • 2.6Previous research on Fusarium spp.
  • 2.7Enzyme activity assays
  • 2.8Factors affecting enzyme activity
  • 2.9Applications of ∞-amylase
  • 2.10Future trends in enzyme research

Chapter THREE

RESEARCH METHODOLOGY

  • 3.1Research design
  • 3.2Sampling techniques
  • 3.3Data collection methods
  • 3.4Experimental setup
  • 3.5Data analysis techniques
  • 3.6Ethical considerations
  • 3.7Reliability and validity
  • 3.8Research limitations

Chapter FOUR

DATA PRESENTATION AND ANALYSIS

  • 4.1Overview of findings
  • 4.2Analysis of results
  • 4.3Comparison with existing literature
  • 4.4Interpretation of data
  • 4.5Discussion of significant findings
  • 4.6Implications of findings
  • 4.7Recommendations for future research
  • 4.8Conclusion

Chapter FIVE

SUMMARY, CONCLUSION AND RECOMMENDATIONS

  • 5.1Summary of research
  • 5.2Conclusion
  • 5.3Implications of the study
  • 5.4Recommendations
  • 5.5Future research directions

Thesis Abstract

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.

Thesis Overview

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