Please wait a minute...

中国生物工程杂志

China Biotechnology
China Biotechnology  2013, Vol. 33 Issue (5): 81-85    DOI:
    
Influence of PEG to ELP[I]40 Inverse Temperature Transition
LIN Heng1,2, LI Jun-ming2, GE Gao-shun2, ZHANG Li-chao2, SUN Li-hui2, HU Xue-jun2
1. College of Life Science and Technology, Dalian University, Dalian 116622, China;
2. Medical College, Dalian University, Dalian 116622, China
Download: HTML   PDF(481KB) HTML
Export: BibTeX | EndNote (RIS)      

Abstract  Objective: To study PEG on the influence of ELP[I]40 inverse temperature transition (Tt). Methods: The ELP[I]40 gene (a (VPGIG)40 five peptide unit composition) was designed and synthesised, and it was expressed and purified, then the Tt was detected under the condition of different concentrations of PEG. Results: In the ELP 40 final concentration to 25 μmol/L, when PEG concentration was 5%, 10%, 15%, 20%, 25%, theTt was respectively reduced down to 26.5℃ and 22℃, 15.2℃, 8.8℃, 2.5℃ from 29℃. Conclusion: The PEG can enhance the ELP purification efficiency via reducing the Tt.

Key wordsPEG Elastin-like polypeptide tag      Inverse temperature transition      Purification     
Received: 04 January 2013      Published: 25 May 2013
ZTFLH:  Q51  
Cite this article:

LIN Heng, LI Jun-ming, GE Gao-shun, ZHANG Li-chao, SUN Li-hui, HU Xue-jun. Influence of PEG to ELP[I]40 Inverse Temperature Transition. China Biotechnology, 2013, 33(5): 81-85.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2013/V33/I5/81

[1] MacEwan S R, Chilkoti A. Elastin-like polypeptides: biomedical applications of tunable biopolymers. Biopolymers, 2010, 94(1): 60-77.
[2] Meyer D E, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol, 1999, 17(11): 1112-1115.
[3] 黄凯宗, 王文研, 张光亚. 类弹性蛋白多肽及其在生物医学材料的应用. 中国生物工程杂志, 2010, 30(5): 128-132. Huang K Z, Wang W Y, Zhang G Y. Advances in applications of elastin-like polypeptides in biomedical materials. China Biotechnology, 2010, 30(5): 128-132.
[4] Lim D W, Trabbic-Carlson K, Mackay J A, et al. Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides. Biomacromolecules, 2007, 8(5): 1417-1424.
[5] 黄凯宗, 李晶晶, 李巍, 等. 类弹性蛋白多肽的从头设计、非色谱纯化及盐效应. 生物工程学报, 2011, 27(4): 653-658. Huang K Z, Li J J, Li W, et al. De novo design, non-chromatographic purification and salt-effect of elastin-like polypeptides. Chin J Biotech, 2011, 27(4): 653-658.
[6] Albertsson P A, Frick G. Partition of virus particles in a liquid two-phase system. Biochim Biophys Acta, 1960, 15(37): 230-237.
[7] Alberts B M. Efficient separation of single-stranded and double-stranded deoxyribonucleic acid in a dextran-polyethylene glycol two-phase system. Biochemistry, 1967, 6(8): 2527-2532.
[8] Coelho D F, Silveira E, Pessoa Junior A, et al. Bromelain purification through unconventional aqueous two-phase system (PEG/ammonium sulphate). Bioprocess Biosyst Eng, 2013,36(2):185-192.
[9] 王伟楠, 赵雨, 李红艳, 等. 人参蛋白四种提取方法的比较研究. 食品工业科技, 2010, 31(5): 280-281. Wang W N, Zhao Y, Li H Y, et al. Study on comparison of four kinds of extracting methods of ginseng protein. Science and Technology of Food Industry, 2010, 31(5): 280-281.
[10] Hart D S, Gehrke S H. Thermally associating polypeptides designed for drug delivery produced by genetically engineered cells. J Pharm Sci, 2007, 96(3): 484-516.
[11] 王建龙, 文湘华. 现代环境生物技术. 北京: 清华大学出版社, 2001: 46-47. Wang J L, Wen X H. Modern Environmental Biological Technology. Beijing: Tsinghua University Press, 2001: 46-47.
[12] Banki M R, Feng L, Wood D W. Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat Methods, 2005, 2(9): 659-661.
[13] Meyer D E, Chilkoti A. Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system. Biomacromolecules, 2002, 3(2): 357-367.
[14] 林衡, 李军明, 张立超, 等. 疏水性ELP基因设计与基因库构建. 微生物学通报, 2013, 40(4): 584-592. Lin H, Li J M, Zhang L C, et al. Design and construction of hydrophobic ELP genes library. Microbiology China, 2013, 40(4): 584-592.
[1] ZHANG Ling,CAO Xiao-dan,YANG Hai-xu,LI Wen-lei. The Application of Continuous Purification in Affinity Chromatography and Evaluation of Production Scale-up[J]. China Biotechnology, 2021, 41(6): 38-44.
[2] LV Yi-fan,LI Geng-dong,XUE Nan,LV Guo-liang,SHI Shao-hui,WANG Chun-sheng. Prokaryotic Expression, Purification of LbCpf1 Protein Gene and in Vitro Cleavage Activity Assay[J]. China Biotechnology, 2020, 40(8): 41-48.
[3] JIANG Dan-dan,WANG Yun-long,LI Yu-lin,Zhang Yi-qing. Study on the Delivery of RGD Modified Virus-Like Particles to ICG Targeted Tumors[J]. China Biotechnology, 2020, 40(7): 22-29.
[4] XIE Hang-hang,BAI Hong-mei,YE Chao,CHEN Yong-jun,YUAN Ming-cui,MA Yan-bing. The Purification Procedure for the Recombinant HBcAg Virus-like Particle Easy to Generate Aggregation[J]. China Biotechnology, 2020, 40(5): 40-47.
[5] WEI Wei,CHANG Bao-gen,WANG Ying,LU Fu-ping,LIU Fu-feng. Heterologous Expression, Purification and Aggregation Characterization of Tau Core Fragment 306-378[J]. China Biotechnology, 2020, 40(5): 22-29.
[6] LIU Zhen-zhen,TIAN Da-yong. Development of Sucrose Density Gradient Centrifugation Purification Process for Rabies Vaccine[J]. China Biotechnology, 2020, 40(4): 25-33.
[7] ZHU Tong-tong,YANG Lei,LIU Ying-bao,SUN Wen-xiu,ZHANG Xiu-guo. Purification and Crystallization of PcCRN20-C from Phytophthora capsici[J]. China Biotechnology, 2020, 40(1-2): 116-123.
[8] PAN Bing-jv,ZHANG Wan-yi,SHEN Hui-tao,LIU Ting-ting,LI Zhong-yuan,LUO Xue-gang,SONG Ya-jian. Research Progress on Separation and Purification of Mannan Oligosaccharide[J]. China Biotechnology, 2020, 40(11): 90-95.
[9] Yu-feng XIE,Xue-mei HAN,Fu-ping LU. Expression, Purification and Enzymatic Properties of β-glucosidase from Lactobacillus paracasei[J]. China Biotechnology, 2019, 39(5): 72-79.
[10] JING Jia-mei,XUN Xin,WANG Min,PENG Ru-chao,SHI Yi. Expression and Purification of C-terminal of Arenavirus Polymerase and Screening of Crystallization Conditions[J]. China Biotechnology, 2019, 39(12): 18-23.
[11] ZHU Meng-lu,WANG Xue-yu,LIU Xin,LU Fu-ping,SUN Deng-yue,QIN Hui-min. Heterologous Expression, Purification and Enzymatic Properties of a Novel Leucine 5-Hydroxylase[J]. China Biotechnology, 2019, 39(12): 24-34.
[12] Chao-di TONG,Jian-ping WU,Li-rong YANG,Gang XU. Crystal Structural Analysis of DehDIV-R by X-ray Crystallography[J]. China Biotechnology, 2018, 38(8): 19-25.
[13] Jun-jun CHEN,Ying LOU,Yuan-xing ZHANG,Qin LIU,Xiao-hong LIU. Expression and Purification of Proliferating Cell Nuclear Antigen in Spodoptera frugiperda Cells[J]. China Biotechnology, 2018, 38(7): 14-20.
[14] Shi-jie LI,Yan-kun YANG,Meng LIU,Zhong-hu BAI,Jian JIN. Efficient Expression of SUMO Protease Ulp1 and Used to Express and Purified scFv by His-SUMO tag[J]. China Biotechnology, 2018, 38(3): 51-61.
[15] Yuan-qiao CHEN,Ding-pei LONG,Xiao-xue DOU,Run QI,Ai-chun ZHAO. Studies on the Protein Purification Ability of an ELP30-Tag in Prokaryotic Expression System[J]. China Biotechnology, 2018, 38(2): 54-60.