Purity and concentration of solubilized inclusion bodies in protein refolding

Solubilized inclusion bodies (IBs) refolding process under low protein purity and high protein concentration conditions always re-aggregate targeted functional protein which is not applicable in nanobiotechnology and molecular biology applications. Enhanced green fluorescent protein (EGFP) IBs was u...

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Main Authors:	Chun, Yi Leong, Chua, Gek Kee, Rozaimi, Abu Samah, Chew, Few Ne
Format:	Conference or Workshop Item
Language:	English
Published:	2016
Subjects:	TP Chemical technology
Online Access:	http://umpir.ump.edu.my/id/eprint/17073/ http://umpir.ump.edu.my/id/eprint/17073/1/Purity%20and%20concentration%20of%20solubilized%20inclusion%20bodies.pdf

id	ump-17073
recordtype	eprints
spelling	ump-170732018-08-06T03:08:30Z http://umpir.ump.edu.my/id/eprint/17073/ Purity and concentration of solubilized inclusion bodies in protein refolding Chun, Yi Leong Chua, Gek Kee Rozaimi, Abu Samah Chew, Few Ne TP Chemical technology Solubilized inclusion bodies (IBs) refolding process under low protein purity and high protein concentration conditions always re-aggregate targeted functional protein which is not applicable in nanobiotechnology and molecular biology applications. Enhanced green fluorescent protein (EGFP) IBs was used as the model protein in this study for investigating the effects of protein purity and concentration on the protein refolding process. Three different conditions of solubilized EGFP-IBs were self-refolded at 4°C: solubilized EGFP-IBs with cell debris; solubilized EGFP-IBs after detergent washing; and the purified solubilized EGFP-IBs by using preparative native urea polyacrylamide gel electrophoresis (PAGE). High protein concentration and low protein purity in first and second refolding conditions have resulted reaggregation of solubilized EGFP-IBs. Large molecular structure of self-refolded EGFP were formed and stuck at the top of stacking and resolving gels during the native PAGE protein analysis. The preparative native urea PAGE has successfully clarified and purified the solubilised EGFP-IBs. The result showed that hjgh purity and low concentration of solubilized EGFP-IBs were able to self-refolded correctly. The structure and biological activity of self-refolded EGFP are preserved and has potential to be used in nanobiotechnologies. 2016 Conference or Workshop Item NonPeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/17073/1/Purity%20and%20concentration%20of%20solubilized%20inclusion%20bodies.pdf Chun, Yi Leong and Chua, Gek Kee and Rozaimi, Abu Samah and Chew, Few Ne (2016) Purity and concentration of solubilized inclusion bodies in protein refolding. In: The International Conference on Bioscience and Medical Engineering (ICBME) 2016, 10 October 2016 , Universiti Teknologi Malaysia, Faculty of Bioscience & Medical Engineering. . (Unpublished)
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 Chun, Yi Leong Chua, Gek Kee Rozaimi, Abu Samah Chew, Few Ne Purity and concentration of solubilized inclusion bodies in protein refolding
description	Solubilized inclusion bodies (IBs) refolding process under low protein purity and high protein concentration conditions always re-aggregate targeted functional protein which is not applicable in nanobiotechnology and molecular biology applications. Enhanced green fluorescent protein (EGFP) IBs was used as the model protein in this study for investigating the effects of protein purity and concentration on the protein refolding process. Three different conditions of solubilized EGFP-IBs were self-refolded at 4°C: solubilized EGFP-IBs with cell debris; solubilized EGFP-IBs after detergent washing; and the purified solubilized EGFP-IBs by using preparative native urea polyacrylamide gel electrophoresis (PAGE). High protein concentration and low protein purity in first and second refolding conditions have resulted reaggregation of solubilized EGFP-IBs. Large molecular structure of self-refolded EGFP were formed and stuck at the top of stacking and resolving gels during the native PAGE protein analysis. The preparative native urea PAGE has successfully clarified and purified the solubilised EGFP-IBs. The result showed that hjgh purity and low concentration of solubilized EGFP-IBs were able to self-refolded correctly. The structure and biological activity of self-refolded EGFP are preserved and has potential to be used in nanobiotechnologies.
format	Conference or Workshop Item
author	Chun, Yi Leong Chua, Gek Kee Rozaimi, Abu Samah Chew, Few Ne
author_facet	Chun, Yi Leong Chua, Gek Kee Rozaimi, Abu Samah Chew, Few Ne
author_sort	Chun, Yi Leong
title	Purity and concentration of solubilized inclusion bodies in protein refolding
title_short	Purity and concentration of solubilized inclusion bodies in protein refolding
title_full	Purity and concentration of solubilized inclusion bodies in protein refolding
title_fullStr	Purity and concentration of solubilized inclusion bodies in protein refolding
title_full_unstemmed	Purity and concentration of solubilized inclusion bodies in protein refolding
title_sort	purity and concentration of solubilized inclusion bodies in protein refolding
publishDate	2016
url	http://umpir.ump.edu.my/id/eprint/17073/ http://umpir.ump.edu.my/id/eprint/17073/1/Purity%20and%20concentration%20of%20solubilized%20inclusion%20bodies.pdf
first_indexed	2023-09-18T22:23:18Z
last_indexed	2023-09-18T22:23:18Z
_version_	1777415800735399936

Purity and concentration of solubilized inclusion bodies in protein refolding

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