MARC details
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04599ntm a2200373 i 4500 |
| 003 - CONTROL NUMBER IDENTIFIER |
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MY-KuUP |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
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20251125105422.0 |
| 006 - FIXED-LENGTH DATA ELEMENTS--ADDITIONAL MATERIAL CHARACTERISTICS |
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t||||fr|||| 000 0 |
| 007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION |
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ta |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
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191108t20192019my a|||fram|| 000 0 eng d |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER |
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| International Standard Book Number |
THE0008406(Local) |
| Qualifying information |
hardback |
| 040 ## - CATALOGING SOURCE |
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| Original cataloging agency |
UMP |
| Language of cataloging |
eng |
| Transcribing agency |
UMP |
| Description conventions |
rda |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) |
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| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) |
FKKSA .N38 2019 r Thesis |
| 100 0# - MAIN ENTRY--PERSONAL NAME |
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| Personal name |
Natassha Jamil, |
| Relator term |
author. |
| 245 10 - TITLE STATEMENT |
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| Title |
Immobilization of cyclodextrin glucanotransferase on polyvinylidene fluoride hollow fiber membrane for cyclodextrin production / |
| Statement of responsibility, etc. |
Natassha Jamil |
| 264 ## - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
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| Place of production, publication, distribution, manufacture |
Kuantan, Pahang : |
| Name of producer, publisher, distributor, manufacturer |
UMP, |
| Date of production, publication, distribution, manufacture, or copyright notice |
2019 |
| 264 ## - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
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| Date of production, publication, distribution, manufacture, or copyright notice |
© 2019 |
| 300 ## - PHYSICAL DESCRIPTION |
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| Extent |
xiv, 110 pages : |
| Other physical details |
illustrations ; |
| Dimensions |
30 cm. + |
| Accompanying material |
1 CD-ROM |
| 336 ## - CONTENT TYPE |
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| Content type term |
text |
| Source |
rdacontent |
| 336 ## - CONTENT TYPE |
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| Content type term |
text |
| Source |
rdacontent |
| 337 ## - MEDIA TYPE |
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| Media type term |
unmediated |
| Source |
rdamedia |
| 337 ## - MEDIA TYPE |
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| Media type term |
computer |
| Source |
rdamedia |
| 338 ## - CARRIER TYPE |
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| Carrier type term |
volume |
| Source |
rdacarrier |
| 338 ## - CARRIER TYPE |
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| Carrier type term |
computer disc |
| Source |
rdacarrier |
| 347 ## - DIGITAL FILE CHARACTERISTICS |
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| File type |
text file |
| Encoding format |
PDF |
| Source |
rda |
| 500 ## - GENERAL NOTE |
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| General note |
Faculty of Chemical and Natural Resources Engineering |
| 502 ## - DISSERTATION NOTE |
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| Dissertation note |
Thesis (Master of Science) -- Universiti Malaysia Pahang – 2019 |
| 504 ## - BIBLIOGRAPHY, ETC. NOTE |
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| Bibliography, etc. note |
Includes bibliographical references |
| 520 3# - SUMMARY, ETC. |
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| Summary, etc. |
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. |
| 610 20 - SUBJECT ADDED ENTRY--CORPORATE NAME |
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| Corporate name or jurisdiction name as entry element |
Faculty of Chemical and Natural Resources Engineering |
| General subdivision |
Dissertations |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
Universities and colleges |
| General subdivision |
Disertations |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
Theses |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) |
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| Source of classification or shelving scheme |
Library of Congress Classification |
| Koha item type |
Thesis |