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

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

 

Table Of Contents


Chapter ONE

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

Chapter TWO

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

Chapter THREE

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

Chapter FOUR

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

Chapter FIVE

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

Project 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.

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