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 Sources of ∞-Amylase
2.3 Enzyme Production by Fusarium spp.
2.4 Sweet Potato (Ipomoea batatas) Starch
2.5 Properties of ∞-Amylase from Fusarium spp.
2.6 Applications of ∞-Amylase in Industries
2.7 Factors Affecting ∞-Amylase Activity
2.8 Enzyme Kinetics of ∞-Amylase
2.9 Immobilization Techniques for ∞-Amylase
2.10 Recent Research Trends in ∞-Amylase Studies

Chapter THREE

3.1 Research Methodology Overview
3.2 Selection of Fusarium spp. Strains
3.3 Isolation and Screening of ∞-Amylase
3.4 Enzyme Production and Optimization
3.5 Purification Techniques
3.6 Enzyme Assays and Activity Determination
3.7 Characterization of ∞-Amylase
3.8 Statistical Analysis of Data

Chapter FOUR

4.1 Analysis of Enzyme Production Results
4.2 Purification Yield and Techniques
4.3 Enzyme Kinetics Analysis
4.4 Comparison with Other ∞-Amylase Sources
4.5 Industrial Applications and Feasibility
4.6 Future Research Directions
4.7 Discussion on Enzyme Stability
4.8 Interpretation of Findings

Chapter FIVE

5.1 Summary of Findings
5.2 Conclusions
5.3 Recommendations for Future Research
5.4 Implications of the Study
5.5 Contribution to Existing Knowledge

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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