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008			191108t20192019my a|||fram|| 000 0 eng d
020			_aTHE0008406(Local) _qhardback
040			_aUMP _beng _cUMP _erda
090			_aFKKSA .N38 2019 r Thesis
100	0		_aNatassha Jamil, _eauthor.
245	1	0	_aImmobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production / _cNatassha Jamil
264			_aKuantan, Pahang : _bUMP, _c2019
264			_c© 2019
300			_axiv, 110 pages : _billustrations ; _c30 cm. + _e1 CD-ROM
336			_atext _2rdacontent
336			_atext _2rdacontent
337			_aunmediated _2rdamedia
337			_acomputer _2rdamedia
338			_avolume _2rdacarrier
338			_acomputer disc _2rdacarrier
347			_atext file _bPDF _2rda
500			_aFaculty of Chemical and Natural Resources Engineering
502			_aThesis (Master of Science) -- Universiti Malaysia Pahang – 2019
504			_aIncludes bibliographical references
520	3		_aCyclodextrin glucanotransferase (CGTase) is a multifunctional industrial enzyme that undergoes cyclization reaction to converts starch into cyclodextrin (CD). CD is a non-reducing maltooligosaccharides with a hydrophobic inside and hydrophilic surface outside. With these properties, CD able to form inclusion complexes with many hydrophobic molecules, changing their physical and chemical properties. Due to their potential properties, CD has been discovered to have numerous application in food industries, pharmaceutical, agricultural and environmental engineering. However, the instability of the enzyme during the reaction process resulted in the low production of CD. Therefore, enzyme immobilization technique is a promising solution to improve the enzyme stability in order to achieve high production of CD. The aims of this study are to optimize the immobilization of CGTase on polyvinylidene fluoride (PVDF) hollow fiber membrane by manipulating the immobilization parameters and to investigate the performance of the immobilized enzyme compared to the free CGTase on CD production. In the present study, one-factor-at-one-time (OFAT), fractional factorial design (FFD) and central composite design (CCD) were employed to screen and optimize the effect of immobilization conditions towards the immobilization yields. The reusability and kinetic study of the immobilized enzyme were also performed in order to study the performance of the immobilized CGTase. The free CGTase from Bacillus licheniformis was characterized to determine their optimum temperature and pH for CD production. The enzymatic activity was highest at the temperature of 40 °C and pH 6.0. Immobilization of CGTase on the PVDF hollow fiber membrane was successfully performed via adsorption technique. The effects of enzyme concentration, temperature, agitation rate, contact time and pH on the enzyme immobilization yield were investigated by OFAT method. The immobilized CGTase exhibited an immobilization yield of 19.21% under the conditions of 100 U of enzyme concentration, 25 °C of immobilization temperature, 100 rpm of agitation rate, 24 h contact time and pH 4.0. The immobilization of CGTase on hollow fiber membrane was further optimized by using response surface methodology (RSM). Under the optimized conditions [100 U of enzyme concentration, 24 °C of immobilization temperature, 100 rpm of agitation, 24 h of contact time and pH 6.7], 88.25% of CGTase immobilization yield was recorded. This illustrated that 4.6-fold increment of the immobilization yield was achieved compared to before optimization process. The reusability of the immobilized CGTase revealed that the immobilized enzyme could retain 37.7% of its initial activity after 10 cycles of reusability. The cumulative production of CD by the immobilized CGTase after 10 cycles was 26.43 mg/ml. The kinetic study of the immobilized and free CGTase discovered that the immobilization process not relatively altered the intrinsic characteristic of the enzyme, suggesting that the hollow fiber membrane appeared as a suitable support for enzyme immobilization system. Hence, immobilization of CGTase on the hollow fiber membrane substantially improved the production of CD by allowing the reusability of the enzyme.
610	2	0	_aFaculty of Chemical and Natural Resources Engineering _xDissertations
650		0	_aUniversities and colleges _xDisertations
650		0	_aTheses
942			_2lcc _cTHESIS