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
- 2.3Enzyme Production by Fusarium spp.
- 2.4Sweet Potato (Ipomoea batatas) Starch
- 2.5Properties of ∞-Amylase from Fusarium spp.
- 2.6Applications of ∞-Amylase in Industries
- 2.7Factors Affecting ∞-Amylase Activity
- 2.8Enzyme Kinetics of ∞-Amylase
- 2.9Immobilization Techniques for ∞-Amylase
- 2.10Recent Research Trends in ∞-Amylase Studies
Chapter THREE
RESEARCH METHODOLOGY
- 3.1Research Methodology Overview
- 3.2Selection of Fusarium spp. Strains
- 3.3Isolation and Screening of ∞-Amylase
- 3.4Enzyme Production and Optimization
- 3.5Purification Techniques
- 3.6Enzyme Assays and Activity Determination
- 3.7Characterization of ∞-Amylase
- 3.8Statistical Analysis of Data
Chapter FOUR
DATA PRESENTATION AND ANALYSIS
- 4.1Analysis of Enzyme Production Results
- 4.2Purification Yield and Techniques
- 4.3Enzyme Kinetics Analysis
- 4.4Comparison with Other ∞-Amylase Sources
- 4.5Industrial Applications and Feasibility
- 4.6Future Research Directions
- 4.7Discussion on Enzyme Stability
- 4.8Interpretation of Findings
Chapter FIVE
SUMMARY, CONCLUSION AND RECOMMENDATIONS
- 5.1Summary of Findings
- 5.2Conclusions
- 5.3Recommendations for Future Research
- 5.4Implications of the Study
- 5.5Contribution 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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