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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| Format: | Conference or Workshop Item |
| Language: | English |
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2016
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| 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 |
| _version_ | 1848820338891161600 |
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| 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 |
| building | UMP Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T02:07:52Z |
| format | Conference or Workshop Item |
| id | ump-17073 |
| institution | Universiti Malaysia Pahang |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T02:07:52Z |
| publishDate | 2016 |
| recordtype | eprints |
| repository_type | Digital Repository |
| 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) (Unpublished) |
| 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 |
| title | 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_short | Purity and concentration of solubilized inclusion bodies in protein refolding |
| title_sort | purity and concentration of solubilized inclusion bodies in protein refolding |
| topic | TP Chemical technology |
| 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 |