Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production

Cyclodextrin 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...

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Main Author:	Natassha, Jamil
Format:	Thesis
Language:	English
Published:	2019
Subjects:	Q Science (General) TP Chemical technology
Online Access:	http://umpir.ump.edu.my/id/eprint/29029/1/Immobilization%20of%20cyclodextrin%20glucanotransferase%20on%20polyvinylidene%20fluoride%20hollow%20fiber%20membrane.pdf
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spelling	my-ump-ir.290292020-08-18T03:37:55Z Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production 2019-01 Natassha, Jamil Q Science (General) TP Chemical technology Cyclodextrin 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. 2019-01 Thesis http://umpir.ump.edu.my/id/eprint/29029/ http://umpir.ump.edu.my/id/eprint/29029/1/Immobilization%20of%20cyclodextrin%20glucanotransferase%20on%20polyvinylidene%20fluoride%20hollow%20fiber%20membrane.pdf pdf en public masters Universiti Malaysia Pahang Faculty of Chemical & Natural Resources Engineering
institution	Universiti Malaysia Pahang Al-Sultan Abdullah
collection	UMPSA Institutional Repository
language	English
topic	Q Science (General) TP Chemical technology
spellingShingle	Q Science (General) TP Chemical technology Natassha, Jamil Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
description	Cyclodextrin 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.
format	Thesis
qualification_level	Master's degree
author	Natassha, Jamil
author_facet	Natassha, Jamil
author_sort	Natassha, Jamil
title	Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
title_short	Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
title_full	Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
title_fullStr	Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
title_full_unstemmed	Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
title_sort	immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production
granting_institution	Universiti Malaysia Pahang
granting_department	Faculty of Chemical & Natural Resources Engineering
publishDate	2019
url	http://umpir.ump.edu.my/id/eprint/29029/1/Immobilization%20of%20cyclodextrin%20glucanotransferase%20on%20polyvinylidene%20fluoride%20hollow%20fiber%20membrane.pdf
_version_	1783732115024642048

Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production

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