Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1

Background The fermentation conditions of recombinant maltose-binding protein fused to neutrophil-activating protein (rMBP-NAP) of Helicobacter pylori were optimized from Escherichia coli TB1 with varying medium, inoculum age and size, time, inducer, pH and temperature in batch fermentation. Results...

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Autores principales:	Lu,Jike, Song,Qi, Ji,Zhenyu, Liu,Xin, Wang,Ting, Kang,Qiaozhen
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2015
Materias:	Escherichia coli Fermentation Optimization Recombinant protein
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000400004
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spelling	oai:scielo:S0717-345820150004000042015-12-04Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1Lu,JikeSong,QiJi,ZhenyuLiu,XinWang,TingKang,Qiaozhen Escherichia coli Fermentation Optimization Recombinant protein Background The fermentation conditions of recombinant maltose-binding protein fused to neutrophil-activating protein (rMBP-NAP) of Helicobacter pylori were optimized from Escherichia coli TB1 with varying medium, inoculum age and size, time, inducer, pH and temperature in batch fermentation. Results It was revealed that the optimal conditions for the production of rMBP-NAP in shake flask were as follows: M9 medium (with 3% yeast extract powder added), inoculum age of 19 h, inoculum size of 6%, initial pH of 6.6, temperature of 37°C, and 0.7 mmoL/L IPTG inducted 21 h in a 50 mL/250 mL shake flask. The recombinant protein yield was increased from 59 to 592 mg/L after optimization. Fermentation process conducted in a 10 L fermenter with similar conditions could get 30 g/L wet cell and 1.738 g/L soluble protein with the rMBP-NAP expression level of 11.9%. Conclusion The results improve the expression level of rMBP-NAP, and it is expected that these optimized conditions can be well applied for large scale production of rMBP-NAP.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.18 n.4 20152015-07-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000400004en10.1016/j.ejbt.2015.05.002
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Escherichia coli Fermentation Optimization Recombinant protein
spellingShingle	Escherichia coli Fermentation Optimization Recombinant protein Lu,Jike Song,Qi Ji,Zhenyu Liu,Xin Wang,Ting Kang,Qiaozhen Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
description	Background The fermentation conditions of recombinant maltose-binding protein fused to neutrophil-activating protein (rMBP-NAP) of Helicobacter pylori were optimized from Escherichia coli TB1 with varying medium, inoculum age and size, time, inducer, pH and temperature in batch fermentation. Results It was revealed that the optimal conditions for the production of rMBP-NAP in shake flask were as follows: M9 medium (with 3% yeast extract powder added), inoculum age of 19 h, inoculum size of 6%, initial pH of 6.6, temperature of 37°C, and 0.7 mmoL/L IPTG inducted 21 h in a 50 mL/250 mL shake flask. The recombinant protein yield was increased from 59 to 592 mg/L after optimization. Fermentation process conducted in a 10 L fermenter with similar conditions could get 30 g/L wet cell and 1.738 g/L soluble protein with the rMBP-NAP expression level of 11.9%. Conclusion The results improve the expression level of rMBP-NAP, and it is expected that these optimized conditions can be well applied for large scale production of rMBP-NAP.
author	Lu,Jike Song,Qi Ji,Zhenyu Liu,Xin Wang,Ting Kang,Qiaozhen
author_facet	Lu,Jike Song,Qi Ji,Zhenyu Liu,Xin Wang,Ting Kang,Qiaozhen
author_sort	Lu,Jike
title	Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
title_short	Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
title_full	Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
title_fullStr	Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
title_full_unstemmed	Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1
title_sort	fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from escherichia coli tb1
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2015
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000400004
work_keys_str_mv	AT lujike fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1 AT songqi fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1 AT jizhenyu fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1 AT liuxin fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1 AT wangting fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1 AT kangqiaozhen fermentationoptimizationofmaltosebindingproteinfusedtoneutrophilactivatingproteinfromescherichiacolitb1
_version_	1718441911977508864

Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1

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