Home / Biology edcuation / 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 Sources of ∞-Amylase
2.3 Enzyme Activity
2.4 Production of ∞-Amylase
2.5 Properties of ∞-Amylase
2.6 Applications of ∞-Amylase
2.7 Factors Affecting ∞-Amylase Activity
2.8 Enzyme Kinetics
2.9 Enzyme Assays
2.10 Industrial Uses of ∞-Amylase

Chapter THREE

3.1 Research Methodology Overview
3.2 Research Design
3.3 Sampling Techniques
3.4 Data Collection Methods
3.5 Data Analysis Procedures
3.6 Ethical Considerations
3.7 Research Limitations
3.8 Research Validity and Reliability

Chapter FOUR

4.1 Analysis of Data
4.2 Interpretation of Results
4.3 Comparison with Existing Literature
4.4 Discussion of Findings
4.5 Implications of Results
4.6 Recommendations for Future Research
4.7 Practical Applications
4.8 Conclusion

Chapter FIVE

5.1 Summary of Findings
5.2 Conclusion
5.3 Contribution to Knowledge
5.4 Recommendations
5.5 Areas for Future 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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