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008			260713t20252025my a|||fr|||| 000 0 eng d
020			_aTHE0010724 (Local) _qHardback
040			_aUMPSA _beng _cUMPSA _erda
090			_aFTKKP .Y37 2025 r Bc.
100	1		_aYashini Devi A/P Subramaniam, , , _eauthor.
245	1	0	_aLaccase immobilization onto oxidized bacterial cellulose: the effect of oxidant and its oxidation degree analysis / _cYashini Devi A/P Subramaniam
264		1	_aKuantan, Pahang : _bUMPSA, _c2025
264		4	_c© 2025
300			_axv, 58 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		_aLaccases, a subgroup of multicopper oxidases, play a crucial role in biotechnological applications but face limitations such as low stability, poor reusability, and recovery challenges. This study investigates the effects of oxidant to Bacterial Cellulose (BC) weight ratio and sodium periodate (NaIO4) concentration on oxidation degree (OD) and laccase immobilization efficiency to determine best condition for enzyme stability and activity. The results indicate that increasing the oxidant to BC ratio from 0.02:1 to 0.06:1 led to a gradual increase in OD, peaking at 12.3%, while further increments resulted in over oxidation, causing structural degradation and reduced immobilization efficiency. Similarly, NaIO4 concentrations between 0.2% and 0.6% improved enzyme binding by enhancing aldehyde functionalities, but concentrations beyond 0.6% led to excessive oxidation and mass loss, negatively impacting enzyme stability. Under best condition of 0.06:1 oxidant to BC ratio and 0.6% NaIO4 concentration, Oxidized Bacterial Cellulose (OxBC) demonstrated superior immobilization performance, achieving a laccase activity of 0.04 U, with a recovered activity of 0.2%, and bound laccase of 17.0 U/g of support. The aldehyde groups introduced through oxidation facilitated stable covalent binding, significantly improving enzyme retention and reusability. Compared to native BC, OxBC exhibited enhanced immobilization efficiency and structural integrity, making it a promising candidate for industrial enzyme applications. This study provides insight into the relationship between oxidation parameters and immobilization efficiency, contributing to the development of more effective and sustainable enzyme immobilization systems. Future research should explore long term operational stability and scalability of OxBC based immobilization for broader industrial and environmental applications.
610	2	0	_aFaculty of Chemical and Process Engineering Technology _xDissertations
650		0	_aUniversities and colleges _xDissertations
650		0	_aTheses _xDissertations
942			_2lcc _cPSM
999			_c105192 _d105198