03298ntm a2200349 i 4500 MY-KuUP 20260708181320.0 t|||||r|||| 000 0 ta 260708t20252025my a|||fr|||| 000 0 eng d THE0010684 (Local) Hardback UMPSA eng UMPSA rda FTKKP .H85 2025 r Bc. Law, Hui Ping, , , author. Surface modification of glyoxyl-agarose in immobilization of β-glycosidase for sustainable biosurfactant production - effect of modifier’s carbon length and concentration / Law Hui Ping Kuantan, Pahang : UMPSA, 2025 © 2025 xvI, 54 pages : illustrations ; rdacontent text rdamedia unmediated rdacarrier volume rda text file PDF Faculty of Chemical and Process Engineering Technology Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025 Include bibliographical reference Surfactants are key amphiphilic chemicals used in a wide range of industrial applications. However, conventional surfactant manufacture usually causes environmental problems owing to its reliance on petrochemicals. Biosurfactants derived from biological feedstocks offer a sustainable option. This study aims to evaluate the impact of the modifier’s carbon chain length and concentration on the efficiency of enzyme immobilization. Immobilizing enzymes on glyoxyl agarose improves enzyme stability and reusability, which is essential for effective biosurfactant synthesis. The findings showed that altering glyoxyl-agarose with aldehyde modifiers considerably improves enzyme immobilization efficiency and biosurfactant production. Dodecanal-modified beads demonstrated greater mechanical and thermal stability, with the maximum compression strength (rating of 4.93 vs 2.3 for unmodified beads) and decomposition temperature (179.66°C versus 144.07°C for unmodified beads). Surface characterization found that dodecanal-modified beads at 80% concentration exhibited the strongest hydrophobic interaction (0.0644 mg dye/mg bead), resulting in improved enzyme binding and immobilization yields of up to 45%. However, benzaldehyde-modified beads had the greatest enzyme activity, most likely due to their aromatic structure, which allows for robust enzyme-substrate interactions. These findings highlight the importance of modifier carbon chain length and concentration in determining bead characteristics and enzyme immobilization. Optimizing these parameters improves the stability and efficacy of β-glycosidase immobilization, resulting in higher yield and activity of biosurfactants generated by this method. The work emphasizes the potential of glyoxyl agarose modifications in enhancing sustainable biosurfactant synthesis, urging more research into other modifier types and concentrations to maximize efficiency. Faculty of Chemical and Process Engineering Technology Dissertations Universities and colleges Dissertations Theses Dissertations https://umpir.ump.edu.my/id/eprint/47496 lcc PSM 0 0 lcc 0 0 10000 10000 2026-07-08 0 FTKKP .H85 2025 r Bc. T0000042781 2026-07-08 18:13:37 2026-07-08 PSM 105147 105153