Optimizing the expression of a Heterologous chitinase: A study of different promoters

References

• Adrangi S, Faramarzi MA. From bacteria to human: a journey into the world of chitinases. Biotechnol Adv 2013; 31:1786-95; PMID:24095741; https://doi.org/10.1016/j.biotechadv.2013.09.012
   PubMed Web of Science ®Google Scholar
• Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S. Chitinases: an update. J Pharm Bioallied Sci 2013; 5:21-9; PMID:23559820
   PubMedGoogle Scholar
• Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 2009; 37:D233-8; PMID:18838391; https://doi.org/10.1093/nar/gkn663
   PubMed Web of Science ®Google Scholar
• Yang J, Liang L, Li J, Zhang KQ. Nematicidal enzymes from microorganisms and their applications. Appl Microbiol Biotechnol 2013; 97:7081-95; PMID:23832084; https://doi.org/10.1007/s00253-013-5045-0
   PubMed Web of Science ®Google Scholar
• Nagpure A, Choudhary B, Gupta, RK. Chitinases: In agriculture and human healthcare. Crit Rev Biotechnol 2014; 34:215-32; PMID:23859124; https://doi.org/10.3109/07388551.2013.790874
   PubMed Web of Science ®Google Scholar
• Zhang Y, Zhou Z, Liu Y, Cao Y, He S, Huo F, Qin C, Yao B, Ringo E. High-yield production of a chitinase from Aeromonas veronii B565 as a potential feed supplement for warm-water aquaculture. Appl Microbiol Biotechnol 2014; 98:1651-62; PMID:23775269; https://doi.org/10.1007/s00253-013-5023-6
   PubMed Web of Science ®Google Scholar
• Inokuma K, Takano M, Hoshino K. Direct ethanol production from N-acetylglucosamine and chitin substrates by Mucor species. Biochem Eng J 2013; 72:24-32; https://doi.org/10.1016/j.bej.2012.12.009
   Web of Science ®Google Scholar
• Liu L, Yang H, Shin H, Chen RR, Li J, Du G, Chen J. How to achieve high-level expression of microbial enzymes. Strategies and perspectives. Bioengineered 2013; 4:212-23; PMID:23686280; https://doi.org/10.4161/bioe.24761
   PubMed Web of Science ®Google Scholar
• Hannig G, Makrides SC. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol 1998; 16:54-60; PMID:9487731; https://doi.org/10.1016/S0167-7799(97)01155-4
   PubMed Web of Science ®Google Scholar
• Waegeman H, Soetaert W. Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering. J Ind Microbiol Biotechnol 2011; 38:1891-910; PMID:21901404; https://doi.org/10.1007/s10295-011-1034-4
   PubMed Web of Science ®Google Scholar
• Rosano GL, Ceccarelli EA. Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 2014; 5:1-17; PMID:24478763
   PubMed Web of Science ®Google Scholar
• García-Fraga B, da Silva AF, López-Seijas J, Sieiro C. Optimized expression conditions for enhancing production of two recombinant chitinolytic enzymes from different prokaryote domains. Bioprocess Biosyst Eng 2015; 38:2477-86; https://doi.org/10.1007/s00449-015-1485-5
   PubMed Web of Science ®Google Scholar
• Bolotin A, Wincker P, Mauger S, Jaillon O, Malarme K, Weissenbach J, Ehrlich SD, Sorokin A. The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403. Genome Res 2001; 11:731-53; PMID:11337471; https://doi.org/10.1101/gr.GR-1697R
   PubMed Web of Science ®Google Scholar
• Vaaje-Kolstad G, Bunaes AC, Mathiesen G, Eijsink VG. The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of α- and β-chitin. FEBS J 2009; 276:2402-15; PMID:19348025; https://doi.org/10.1111/j.1742-4658.2009.06972.x
   PubMed Web of Science ®Google Scholar
• Keasling JD. Gene-expression tools for the metabolic engineering of bacteria. Trends Biotechnol 1999; 17:452-60; PMID:10511704; https://doi.org/10.1016/S0167-7799(99)01376-1
   PubMed Web of Science ®Google Scholar
• Balbás P. Understanding the art of producing protein and nonprotein molecules in Escherichia coli. Mol Biotechnol 2001; 19:251-67; https://doi.org/10.1385/MB:19:3:251
   PubMed Web of Science ®Google Scholar
• Tolia NH, Joshua-Tor L. Strategies for protein coexpression in Escherichia coli. Nat Methods 2006; 3:55-64; PMID:16369554; https://doi.org/10.1038/nmeth0106-55
   PubMed Web of Science ®Google Scholar
• Rodríguez-Carmona E, Cano-Garrido O, Dragosits M, Maurer M, Mader A, Kunert R, Mattanovich D, Villaverde A, Vázquez F. Recombinant Fab expression and secretion in Escherichia coli continuous culture at medium cell densities: Influence of temperature. Process Biochem 2012; 47:446-52; https://doi.org/10.1016/j.procbio.2011.11.024
   Web of Science ®Google Scholar
• Kane JF, Hartley DL. Properties of recombinant protein containing inclusion bodies in Escherichia coli. Bioprocess Technol 1991; 12:121-45; PMID:1369303
   PubMedGoogle Scholar
• Baig F, Fernando LP, Salazar MA, Powell RR, Bruce TF, Harcum SW. Dynamic transcriptional response of Escherichia coli to inclusion body formation. Biotechnol Bioeng 2014; 111:980-99; PMID:24338599; https://doi.org/10.1002/bit.25169
   PubMed Web of Science ®Google Scholar
• de Marco A. Recombinant polypeptide production in Escherichia coli: towards a rational approach to improve the yields of functional proteins. Microbial Cell Fact 2013; 12:101; https://doi.org/10.1186/1475-2859-12-101
   PubMed Web of Science ®Google Scholar
• Tagkopoulos I. Microbial factories under control: auto-regulatory control through engineered stress-induced feedback. Bioengineered 2013; 4:5-8; PMID:22922761; https://doi.org/10.4161/bioe.21935
   PubMed Web of Science ®Google Scholar
• Marschall L, Sagmeister P, Herwig Ch. Tunable recombinant protein expression in Escherichia coli: enabler for continuous processing? Appl Microb Biotechnol 2016; 100:5719-28; https://doi.org/10.1007/s00253-016-7550-4
   PubMed Web of Science ®Google Scholar
• Sambrook J, Russell DW. 2001. Molecular cloning: A laboratory manual (3rd Ed.). Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
   Google Scholar