Optimization of human interferon gamma production in Escherichia coli by response surface methodology

被引：2

作者：

Balderas Hernandez, Victor E. ^{[1
]}

Paz Maldonado, Luz M. T. ^{[1
]}

Medina Rivero, Emilio ^{[1
]}

Barba de la Rosa, Ana P. ^{[1
]}

Ordonez Acevedo, Leandro G. ^{[1
]}

De Leon Rodriguez, Antonio ^{[1
]}

机构：

[1] Inst Potosino Invest Cient & Tecnol, Div Mol Biol, San Luis Potosi 78216, Mexico

来源：

BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | 2008年 / 13卷 / 01期

关键词：

Escherichia coli BL21-SI; minimum medium; therapeutic protein; synthetic gene;

D O I：

10.1007/s12257-007-0126-5

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];

摘要：

The production of human interferon gamma (hIFN-gamma) using a synthetic gene in Escherichia coli BL21-SI was optimized by response surface methodology (RSM) and a Box-Behnken design. The process variables studied were temperature, biomass concentration at induction time and the NaCl concentration as inducer. According to the Box-Behnken design, a second order response function was developed. The optimal expression conditions were a temperature of 32.6 degrees C, induction biomass of 0.31 g/L and 0.3 M NaCl in minimal medium. The model prediction for the maximum hIFN-gamma production was 77.3 mg/L, which corresponded satisfactorily with the experimental data. The hIFN-gamma concentration attained under optimized conditions was 13-times higher than that obtained using the non-optimized conditions. We conclude that RSM is an effective method for the optimization of recombinant protein expression using synthetic genes in E coli. (c) KSBB.

引用

页码：7 / 13

页数：7

共 38 条

[1]

Modeling and optimization I: Usability of response surface methodology [J].

Bas, Deniz ;

Boyaci, Ismail H. .

JOURNAL OF FOOD ENGINEERING, 2007, 78 (03) :836-845

[2]

An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer [J].

Bhandari, P ;

Gowrishankar, J .

JOURNAL OF BACTERIOLOGY, 1997, 179 (13) :4403-4406

[3]

Production of recombinant serpins in Escherichia coli [J].

Bird, PI ;

Pak, SC ;

Worrall, DM ;

Bottomley, SP .

METHODS, 2004, 32 (02) :169-176

[4]

Box GEP., 1960, TECHNOMETRICS, V2, P455, DOI [10.2307/1266454, DOI 10.1080/00401706.1960.10489912, 10.1080/00401706.1960.10489912]

[5]

Analysis of the expression of the Trichoderma harzianum ech42 gene in two isogenic clones of Escherichia coli by surface response methodology [J].

De León, A ;

Jiménez-Islas, H ;

González-Cuevas, M ;

de la Rosa, APB .

PROCESS BIOCHEMISTRY, 2004, 39 (12) :2173-2178

[6]

Bacterial expression and purification of biologically active mouse c-Fos proteins by selective codon optimization [J].

Deng, TL .

FEBS LETTERS, 1997, 409 (02) :269-272

[7]

HUMAN GAMMA-INTERFERON EXPRESSION IN THE MAMMARY-GLAND OF TRANSGENIC MICE [J].

DOBROVOLSKY, VN ;

LAGUTIN, OV ;

VINOGRADOVA, TV ;

FROLOVA, IS ;

KUZNETSOV, VP ;

LARIONOV, OA .

FEBS LETTERS, 1993, 319 (1-2) :181-184

[8]

Donahue Jr R.A., 1999, FOCUS, V21, P49

[9]

Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter [J].

Donovan, RS ;

Robinson, CW ;

Glick, BR .

JOURNAL OF INDUSTRIAL MICROBIOLOGY, 1996, 16 (03) :145-154

[10]

High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: Evidence for a C-terminal membrane binding domain [J].

Feng, L ;

Chan, WW ;

Roderick, SL ;

Cohen, DE .

BIOCHEMISTRY, 2000, 39 (50) :15399-15409

← 1 2 3 4 →