Abstract
Recombinant human interferon-β (rhIFN-β) is therapeutically important and new commercially viable approaches are needed for its increased production. In this study, a codon-optimized gene encoding for rhIFN-β(C17S) protein was designed and expressed in E. coli SE1. As a first step of medium optimization, growth of E. coli as a function of different media components was studied. Subsequently, to optimize the media composition, a response surface methodology (RSM) was used. Our results show that optimized medium (15.0 g/L tryptone, 12.3 g/L meat extract, 1.0 g/L MgSO4 and 0.5 g/L thiamine along with minimal medium) obtained in this study provide better growth of recombinant cells and the expression level of recombinant protein was ~ 1.7-fold more than Luria–Bertani medium. The optimized medium may be utilized for the large-scale production of rhIFN-β.
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Abbreviations
- CCD:
-
Central composite design
- rhIFN-β(C17S) :
-
Recombinant human interferon-beta variant containing C17S substitution
- PB:
-
Plackett–Burman
- LB medium:
-
Luria–Bertani medium
- RSM:
-
Response surface methodology
- IPTG:
-
Isopropyl-1-thio β-D galactopyranoside
- Cys:
-
Cysteine
References
Agbogbo FK, Ramsey P et al (2020) Upstream, development of Escherichia coli fermentation process with PhoA promoter using design of experiments (DoE). J Ind Microbiol 7:789–799
Arregui MB, Callum GJM et al (2018) Production of biologically active feline interferon beta in insect larvae using a recombinant baculovirus. 3 Biotech 8:341
Babaeipour V, Shojaosadati SA et al (2010) Enhancement of human γ-Interferon production in recombinant E. coli using batch cultivation. Appl Biochem Biotechnol 160:2366–2376
Babaeipour V, Shojaosadati SA et al (2007) Over-production of human interferon-γ by HCDC of recombinant Escherichia coli. Process Biochem 42:112–117
Bey RF, Simonson RR et al (2013) Rotavirus subunit vaccines and methods of making and use there of. WO2013123219A1
Chen X, Li Y et al (2005) Application of response surface methodology in medium optimization for spore production of Coniothyrium minitans in solid-state fermentation. World J Microbiol Biotechnol 21:593–599
Collins T, Barroca MJ et al (2013) Optimising the production of a silk-elastin-like protein in E. coli: overcoming acetate accumulation and plasmid instability. Microbiotec 2013:2013
Fan G, Zhu Y et al (2020) Optimization of fermentation conditions for the production of recombinant feruloyl esterase from Burkholderia pyrrocinia B1213. 3 Biotech 10:216
Fazeli A, Shojaosadati SA et al (2011) Effect of parallel feeding of oxidizing agent and protein on fed-batch refolding process of recombinant interferon beta-1b. Process Biochem 46(3):796–800
Huang C-J, Lin H et al (2012) Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol 39:383–399
Huang C, Feng Y et al (2021) Production, immobilization and characterization of beta-glucosidase for application in cellulose degradation from a novel Aspergillus versicolor. Int J Biol Macromol 177:437–446
Li J, Sun C et al (2017) Optimization of the secretory expression of recombinant human C-reactive protein in Pichia pastoris. 3 Biotech 7:291
Maldonado LMTP, Hernández VEB et al (2007) Optimization of culture conditions for a synthetic gene expression in Escherichia coli using response surface methodology: the case of human interferon beta. Biomol Eng 24:217–222
Mark DF, Lu SD et al (1984) Site-specific mutagenesis of the human fibroblast interferon gene. Proc Natl Acad Sci 81:5662–5666
Morowvat MH, Babaeipour V et al (2015) Optimization of fermentation conditions for recombinant human interferon beta production by Escherichia coli using the response surface methodology. Jundishapur J Microbiol 8(4):e16236
Pal D, Tripathy RK et al (2018) Antibiotic-free expression system for the production of human interferon-beta protein. 3 Biotech 8(1):36
Papaneophytou CP, Kontopidis G (2014) Statistical approaches to maximize recombinant protein expression in Escherichia coli: a general review. Protein Expr Purif 94:22–32
Patel G, Biswas K et al (2018) Bioreactor studies for the growth and production of mycophenolic acid by Penicillium brevicompactum. Biochem Eng J 140:77–84
Patel G, Patil MD et al (2016) Production of mycophenolic acid by Penicillium brevicompactum using solid state fermentation. Appl Biochem Biotechnol 182(1):97–109
Patel G, Khobragade TP et al (2020) Optimization of media and culture conditions for the production of tacrolimus by Streptomyces tsukubaensis in shake flask and fermenter level. Biocatal Agric Biotechnol 29:101803
Patil MD, Dev M (2017) Surfactant-mediated permeabilization of Pseudomonas putida KT2440 and use of the immobilized permeabilized cells in biotransformation. Process Biochem 63:113–121
Patil MD, Shinde KD et al (2016) Use of response surface method for maximizing the production of arginine deiminase by Pseudomonas putida. Biotechnol Rep 10:29–37
Peubez I, Chaudet N et al (2010) Antibiotic-free selection in E. coli: new considerations for optimal design and improved production. Microb Cell Fact 9:65
Poccia ME, Beccaria AJ et al (2014) Modelling the microbial growth of two Escherichia coli strains in a multi-substrate environment. Brazilian J Chem Eng 31:347–354
Qi M, Lu D et al (2014) Antitumor effect of recombinant human interferon-β adenovirus on esophageal squamous cell cancer in vitro. Dis Esophagus 27(2):196–201
Reder AT, Feng X (2014) How type I interferons work in multiple sclerosis and other diseases: some unexpected mechanisms. J Interf Cytokine Res 34:589–599
Rosano GL, Ceccarelli EA (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 5:172
Rudick RA, Goelz SE (2011) Beta-interferon for multiple sclerosis. Exp Cell Res 317:1301–2131
Samarin ZE, Abolghasemi S et al (2018) Response surface optimization of the expression conditions for synthetic human interferon a -2b gene in Escherichia coli. Indian J Pharm Sci 80(3):470–479
Shayesteh M, Ghasemi F et al (2020) Design, construction, and expression of recombinant human interferon beta gene in CHO-s cell line using EBV-based expression system. Res Pharm Sci 15(2):144–153
Shin CS, Hong MS et al (2001) High-level production of recombinant human IFN-α2a with co-expression of tRNA in high-cell-density cultures of Escherichia coli. Biotechnol Bioprocess Eng 6:301–305
Sohoni SV, Nelapati D et al (2015) Optimization of high cell density fermentation process for recombinant nitrilase production in E. coli. Bioresour Technol 188:202–208
Spolaore B, Forzato G et al (2018) Site-specific derivatization of human interferon β-1a at lysine residues using microbial transglutaminase. Amino Acids 7:1–10
Stevens RC, Suzuki SM et al (2008) Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning. Proc Natl Acad Sci 105:12780–12784
Szpirer CY, Milinkovitch MC (2005) Separate-component-stabilization system for protein and DNA production without the use of antibiotics. Biotechniques 38:775–781
Tabandeh F, Khodabandeh M et al (2008) Response surface methodology for optimizing the induction conditions of recombinant interferon beta during high cell density culture. Chem Eng Sci 63:2477–2483
Tripathi NK (2016) Production and purification of recombinant proteins from Escherichia coli. ChemBioEng Rev 3(3):116–133
Zhang Y, Wei X et al (2017) Optimization of culturing conditions of recombined Escherichia coli to produce umami octopeptide-containing protein. Food Chem 227:78–84
Funding
This work was supported in partial by the research grants to AHP from the Department of Biotechnology (New Delhi) (BT/PR23283/MED/30/1953/2018) and NIPER, SAS Nagar (NPLC-AHP). DP and GP are thankful to the University Grants Commission and Department of Biotechnology, New Delhi, Govt. of India for support.
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AHP and UCB were in-charge of the experiments and paper writing. DP, GP and PD performed experimental studies and participated in paper writing. SHN and GP performed review and editing. All the authors read and approved the final manuscript.
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Pal, D., Patel, G., Dobariya, P. et al. Optimization of medium composition to increase the expression of recombinant human interferon-β using the Plackett–Burman and central composite design in E. coli SE1. 3 Biotech 11, 226 (2021). https://doi.org/10.1007/s13205-021-02772-1
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DOI: https://doi.org/10.1007/s13205-021-02772-1