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008			260708t20252025my a|||fr|||| 000 0 eng d
020			_aTHE0010684 (Local) _qHardback
040			_aUMPSA _beng _cUMPSA _erda
090			_aFTKKP .H85 2025 r Bc.
100	1		_aLaw, Hui Ping, , , _eauthor.
245	1	0	_aSurface modification of glyoxyl-agarose in immobilization of β-glycosidase for sustainable biosurfactant production - effect of modifier’s carbon length and concentration / _b _cLaw Hui Ping
264		1	_aKuantan, Pahang : _bUMPSA, _c2025
264		4	_c© 2025
300			_axvI, 54 pages : _billustrations ;
336			_2rdacontent _atext
337			_2rdamedia _aunmediated
338			_2rdacarrier _avolume
347			_2rda _atext file _bPDF
500			_aFaculty of Chemical and Process Engineering Technology
502			_aFinal Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025
504			_aInclude bibliographical reference
520	3		_aSurfactants 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.
610	2	0	_aFaculty of Chemical and Process Engineering Technology _xDissertations
650		0	_aUniversities and colleges _xDissertations
650		0	_aTheses _xDissertations
856			_uhttps://umpir.ump.edu.my/id/eprint/47496
942			_2lcc _cPSM
999			_c105147 _d105153