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Chinese Academy of Sciences Institutional Repositories Grid
Scale-up of fermentation and purification of recombinant allophycocyanin over-expressed in Escherichia coli

文献类型:期刊论文

作者Ge, BS; Tang, ZH; Zhao, FQ; Ren, YH; Yang, Y; Qin, S
刊名PROCESS BIOCHEMISTRY
出版日期2005-10-01
卷号40期号:10页码:3190-3195
关键词Scale-up Recombinant Allophycocyanin Escherichia Coli Protein Purification Tumour Inhibition
ISSN号1359-5113
DOI10.1016/j.procbio.2005.02.023
文献子类Article
英文摘要Phycobiliprotein is a photosynthetic antenna pigment found in cyanobacteria, rhodophytes, cryptophytes and certain dinoflagellates, which has been found to have anti-oxidative and anti-tumour activities. In this paper, a recombinant allophycocyanin (rAPC) had been expressed in Escherichia coli for anti-tumour effect. E. coli cells were cultured using glucose fed-batch method to achieve high cell densities. The biomass of rAPC was up to 3.52 g/L broth. The rAPC was purified from soluble E. coli cell lysate employing hydrophobic interaction chromatographic (HIC) method developed at the bench scale using 20 mL column. The process was performed at the pilot scale using 500 mL column for evaluation of scale-up. An amylose affinity column was used to improve the purity of final product in pilot scale purification. The purification process resulted in greater than 98% pure product and yielded up to 2.0 g/kg wet cells at the bench scale and 1.2 g/kg wet cells at the pilot scale. Peptide mapping was used to prove the identity of rAPC purified from bench scale and pilot scale process. Purified rAPC at the pilot scale was found to have remarkable inhibition on S-180 carcinoma in mice. (c) 2005 Elsevier Ltd. All rights reserved.; Phycobiliprotein is a photosynthetic antenna pigment found in cyanobacteria, rhodophytes, cryptophytes and certain dinoflagellates, which has been found to have anti-oxidative and anti-tumour activities. In this paper, a recombinant allophycocyanin (rAPC) had been expressed in Escherichia coli for anti-tumour effect. E. coli cells were cultured using glucose fed-batch method to achieve high cell densities. The biomass of rAPC was up to 3.52 g/L broth. The rAPC was purified from soluble E. coli cell lysate employing hydrophobic interaction chromatographic (HIC) method developed at the bench scale using 20 mL column. The process was performed at the pilot scale using 500 mL column for evaluation of scale-up. An amylose affinity column was used to improve the purity of final product in pilot scale purification. The purification process resulted in greater than 98% pure product and yielded up to 2.0 g/kg wet cells at the bench scale and 1.2 g/kg wet cells at the pilot scale. Peptide mapping was used to prove the identity of rAPC purified from bench scale and pilot scale process. Purified rAPC at the pilot scale was found to have remarkable inhibition on S-180 carcinoma in mice. (c) 2005 Elsevier Ltd. All rights reserved.
学科主题Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical
URL标识查看原文
语种英语
WOS记录号WOS:000231833100006
公开日期2010-12-22
源URL[http://ir.qdio.ac.cn/handle/337002/3095]  
专题海洋研究所_实验海洋生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式
GB/T 7714
Ge, BS,Tang, ZH,Zhao, FQ,et al. Scale-up of fermentation and purification of recombinant allophycocyanin over-expressed in Escherichia coli[J]. PROCESS BIOCHEMISTRY,2005,40(10):3190-3195.
APA Ge, BS,Tang, ZH,Zhao, FQ,Ren, YH,Yang, Y,&Qin, S.(2005).Scale-up of fermentation and purification of recombinant allophycocyanin over-expressed in Escherichia coli.PROCESS BIOCHEMISTRY,40(10),3190-3195.
MLA Ge, BS,et al."Scale-up of fermentation and purification of recombinant allophycocyanin over-expressed in Escherichia coli".PROCESS BIOCHEMISTRY 40.10(2005):3190-3195.

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来源:海洋研究所

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