Dhashni A/P Guna Segaran, <br/><br/>
Study on the enzyme kinetics of mannanase in poultry feed hydrolysis / 
Dhashni A/P Guna Segaran 
 - xv, 55 pages :  illustrations ; 
<br/><br/> Faculty of Chemical and Process Engineering Technology 
<br/><br/>Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025 
<br/><br/>Include bibliographical reference 
<br/><br/> A typical protein source necessary for our daily nourishment is poultry. Due to increased demand for chicken meat and eggs brought on by population growth, urbanization, industrialization, and greater purchasing power, poultry production has increased globally. Due to poultry lacking the digestive enzymes needed to completely break down fibre, which lowers the growth performance of poultries, their meals have changed from traditional feed to commercial poultry feed with the extra help from the enzymes to improve the digestion viscosity. In this study, the approach will be based on the in-vitro method, where poultry feed was experimented with and not on the animals. Hence, the study is mainly on the enzyme kinetics of mannanase in poultry feed for optimizing its efficiency. Key parameters, such as substrate concentration and pH, directly impact the enzyme's activity and the release of mannose. Enzymes can improve commercial poultry feed formulation by increasing enzyme-substrate binding efficiency when added to the feed under the correct parameters. The main objective of this research is to investigate the enzyme kinetics of commercial mannanase in poultry feed hydrolysis. To investigate the enzyme kinetics of commercial mannanase, experiments were conducted with varying substrate concentrations, pH, and temperature while fixing other conditions to control the substrate usage using the Central Composite Design method. The process involves the reaction of mannanase with poultry feed, followed by the addition of DNS to stop the reaction. A UV-Vis spectrophotometer is then used to measure the solution's absorbance at 540 nm. From the optimum pH and temperature, kinetic parameters are determined by varying the substrate concentration. The ideal pH and temperature are expected to be 6 and 50 ℃, while it is likely that the Km value (0.3609 mg/ml) is lower than the Vmax value (0.0312μmol min-1 mg-1). In conclusion, by identifying the optimal substrate concentration and pH for enzymatic hydrolysis based on the kinetic study, the study established conditions that significantly enhance mannose production, improve nutrient absorption and lead to cost-effectiveness. 
<br/><br/><label>ISBN: </label>THE0010670 (Local) 
<br/><br/><label>Subjects--Corporate Names: </label><br/>Faculty of Chemical and Process Engineering Technology--Dissertations
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