Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design

Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design

Immobilization of cell for enzyme production provides many advantages such as repeated use of cells, capability to separate the cell from the fermentation medium and freedom from toxicity problems. In this study, hollow fiber membrane was used to immobilize Escherichia coli with the intention to imp...

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Main Authors: Rohaida, Che Man, Ahmad Fauzi, Ismail, Nazlee Faisal, Ghazali, Rosli, Md. Illias
Format: Conference or Workshop Item
Language:English
Published: 2014
Subjects:
TP Chemical technology
Online Access:http://umpir.ump.edu.my/id/eprint/6756/
http://umpir.ump.edu.my/id/eprint/6756/1/Improvement_of_Cyclodextrin_Glucanotranferase_%28CGTase%29_Secretion_by_Recombinant_Escherichia_coi_Immobilized_on_Hollow_Fiber_Membrane_using_Full_Factorial_Design.PDF
id ump-6756
recordtype eprints
spelling ump-67562017-10-30T01:58:34Z http://umpir.ump.edu.my/id/eprint/6756/ Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design Rohaida, Che Man Ahmad Fauzi, Ismail Nazlee Faisal, Ghazali Rosli, Md. Illias TP Chemical technology Immobilization of cell for enzyme production provides many advantages such as repeated use of cells, capability to separate the cell from the fermentation medium and freedom from toxicity problems. In this study, hollow fiber membrane was used to immobilize Escherichia coli with the intention to improve secretion of enzymes and increase cell viability. Full factorial design was applied to identify the critical and significant parameters on immobilized cell towards CGTase secretion and cell viability. The parameters involved in this screening study were temperature, inducer concentration, agitation rate, post induction time and pH. The results show that only temperature, inducer concentration and pH have significant effect on immobilized cell for CGTase secretion and cell viability. Under the significant conditions (25°C, 0.005 mM IPTG and pH 9), the secretion of CGTase was 128- fold increased with 90% reduction of cell lysis compared to one factor at a time method. 2014 Conference or Workshop Item PeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/6756/1/Improvement_of_Cyclodextrin_Glucanotranferase_%28CGTase%29_Secretion_by_Recombinant_Escherichia_coi_Immobilized_on_Hollow_Fiber_Membrane_using_Full_Factorial_Design.PDF Rohaida, Che Man and Ahmad Fauzi, Ismail and Nazlee Faisal, Ghazali and Rosli, Md. Illias (2014) Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design. In: International Symposium on Green Manufacturing and Applications, 24-28th June 2014 , Busan, Korea. .
repository_type Digital Repository
institution_category Local University
institution Universiti Malaysia Pahang
building UMP Institutional Repository
collection Online Access
language English
topic TP Chemical technology
spellingShingle TP Chemical technology
Rohaida, Che Man
Ahmad Fauzi, Ismail
Nazlee Faisal, Ghazali
Rosli, Md. Illias
Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
description Immobilization of cell for enzyme production provides many advantages such as repeated use of cells, capability to separate the cell from the fermentation medium and freedom from toxicity problems. In this study, hollow fiber membrane was used to immobilize Escherichia coli with the intention to improve secretion of enzymes and increase cell viability. Full factorial design was applied to identify the critical and significant parameters on immobilized cell towards CGTase secretion and cell viability. The parameters involved in this screening study were temperature, inducer concentration, agitation rate, post induction time and pH. The results show that only temperature, inducer concentration and pH have significant effect on immobilized cell for CGTase secretion and cell viability. Under the significant conditions (25°C, 0.005 mM IPTG and pH 9), the secretion of CGTase was 128- fold increased with 90% reduction of cell lysis compared to one factor at a time method.
format Conference or Workshop Item
author Rohaida, Che Man
Ahmad Fauzi, Ismail
Nazlee Faisal, Ghazali
Rosli, Md. Illias
author_facet Rohaida, Che Man
Ahmad Fauzi, Ismail
Nazlee Faisal, Ghazali
Rosli, Md. Illias
author_sort Rohaida, Che Man
title Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
title_short Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
title_full Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
title_fullStr Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
title_full_unstemmed Improvement of Cyclodextrin Glucanotranferase (CGTase) Secretion by Recombinant Escherichia Coli Immobilized on Hollow Fiber Membrane Using Full Factorial Design
title_sort improvement of cyclodextrin glucanotranferase (cgtase) secretion by recombinant escherichia coli immobilized on hollow fiber membrane using full factorial design
publishDate 2014
url http://umpir.ump.edu.my/id/eprint/6756/
http://umpir.ump.edu.my/id/eprint/6756/1/Improvement_of_Cyclodextrin_Glucanotranferase_%28CGTase%29_Secretion_by_Recombinant_Escherichia_coi_Immobilized_on_Hollow_Fiber_Membrane_using_Full_Factorial_Design.PDF
first_indexed 2023-09-18T22:02:48Z
last_indexed 2023-09-18T22:02:48Z
_version_ 1777414510631452672

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