1. Werpy, T. and G. Petersen, Top Value Added Chemicals from Biomass: Volume I -- Results of Screening for Potential Candidates from Sugars and Synthesis Gas. 2004: United States.
2. Sajid, M., X. Zhao, and D. Liu, Production of 2,5-furandicarboxylic acid (FDCA) from 5-hydroxymethylfurfural (HMF): recent progress focusing on the chemical-catalytic routes. Green Chemistry, 2018. 20(24): p. 5427-5453.
3. van Deurzen, M.P.J., F. van Rantwijk, and R.A. Sheldon, Chloroperoxidase- Catalyzed Oxidation of 5-Hydroxymethylfurfural. Journal of Carbohydrate Chemistry, 1997. 16(3): p. 299-309.
4. Koopman, F., et al., Identification and characterization of the furfural and 5- (hydroxymethyl)furfural degradation pathways of Cupriavidus basilensis HMF14. Proc Natl Acad Sci U S A, 2010. 107(11): p. 4919-24.
5. Van den Oever, M., et al., Bio-based and biodegradable plastics – Facts and Figures. Focus on food packaging in the Netherlands. 2017.
6. Pang, K., R. Kotek, and A. Tonelli, Review of conventional and novel polymerization processes for polyesters. Progress in Polymer Science, 2006. 31(11): p. 1009-1037.
7. Sousa, A.F., et al., New copolyesters derived from terephthalic and 2,5- furandicarboxylic acids: A step forward in the development of biobased polyesters. Polymer, 2013. 54(2): p. 513-519.
8. Zhang, J., et al., Advances in catalytic production of bio-based polyester monomer 2,5-furandicarboxylic acid derived from lignocellulosic biomass. Carbohydrate Polymers, 2015. 130: p. 420-428.
9. Hanke Paul, D., Enzymatic Oxidation Of Hmf. 2009, ARCHER DANIELS MIDLAND CO: WO.
10. Koopman, F., et al., Efficient whole-cell biotransformation of 5- (hydroxymethyl)furfural into FDCA, 2,5-furandicarboxylic acid. Bioresour Technol, 2010. 101(16): p. 6291-6.
11. Wierckx, N., et al., Microbial degradation of furanic compounds: biochemistry, genetics, and impact. Appl Microbiol Biotechnol, 2011. 92(6): p. 1095-105.
12. Tao, F., et al., Novel organic solvent-responsive expression vectors for biocatalysis: application for development of an organic solvent-tolerant biodesulfurizing strain. Bioresour Technol, 2011. 102(20): p. 9380-7.
13. Tao, F., et al., Biodesulfurization in biphasic systems containing organic solvents. Appl Environ Microbiol, 2006. 72(7): p. 4604-9.
74
14. Pinkart, H.C., et al., Cell Envelope Changes in Solvent-Tolerant and Solvent- Sensitive Pseudomonas putida Strains following Exposure to o-Xylene. Appl Environ Microbiol, 1996. 62(3): p. 1129-32.
15. Isken, S. and J.A.M. de Bont, Bacteria tolerant to organic solvents. Extremophiles, 1998. 2(3): p. 229-238.
16. Li, L., et al., A Toluene-tolerant Mutant of Pseudomonas aeruginosa Lacking the Outer Membrane Protein F. Bioscience, Biotechnology, and Biochemistry, 1995. 59(12): p. 2358-2359.
17. Heipieper, H.J., et al., Mechanisms of resistance of whole cells to toxic organic solvents. Trends in Biotechnology, 1994. 12(10): p. 409-415.
18. Sikkema, J., J.A. de Bont, and B. Poolman, Mechanisms of membrane toxicity of hydrocarbons. Microbiol Rev, 1995. 59(2): p. 201-22.
19. Wery, J., et al., An insertion sequence prepares Pseudomonas putida S12 for severe solvent stress. J Biol Chem, 2001. 276(8): p. 5700-6.
20. Kieboom, J., et al., Identification and molecular characterization of an efflux pump involved in Pseudomonas putida S12 solvent tolerance. J Biol Chem, 1998. 273(1): p. 85-91.
21. Hosseini, R., et al., Regulation of solvent tolerance in Pseudomonas putida S12 mediated by mobile elements. Microb Biotechnol, 2017. 10(6): p. 1558-1568.
22. Kieboom, J., et al., Active Efflux of Organic Solvents by Pseudomonas putida S12 Is Induced by Solvents. Journal of Bacteriology, 1998. 180(24): p. 6769- 6772.
23. Reddington, S.C. and M. Howarth, Secrets of a covalent interaction for biomaterials and biotechnology: SpyTag and SpyCatcher. Curr Opin Chem Biol, 2015. 29: p. 94-9.
24. Zakeri, B., et al., Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci U S A, 2012. 109(12): p. E690-7.
25. Dovala, D., et al., Rapid analysis of protein expression and solubility with the SpyTag-SpyCatcher system. Protein Expr Purif, 2016. 117: p. 44-51.
26. Zhang, G., M.B. Quin, and C. Schmidt-Dannert, Self-Assembling Protein Scaffold System for Easy in Vitro Coimmobilization of Biocatalytic Cascade Enzymes. ACS Catalysis, 2018. 8(6): p. 5611-5620.
27. Liu, Z., et al., A novel method for synthetic vaccine construction based on protein assembly. Sci Rep, 2014. 4: p. 7266.
28. Si, M., et al., SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase. PLoS One, 2016. 11(9): p. e0162318.
29. Jung, I.L. and I.G. Kim, Transcription of ahpC, katG, and katE genes in Escherichia coli is regulated by polyamines: polyamine-deficient mutant sensitive to H2O2-induced oxidative damage. Biochemical and Biophysical Research Communications, 2003. 301(4): p. 915-922.
30. Miller, C.D., Y.C. Kim, and A.J. Anderson, Cloning and mutational analysis of the gene for the stationary-phase inducible catalase (catC) from Pseudomonas putida. J Bacteriol, 1997. 179(16): p. 5241-5.
31. Hillar, A., L. Van Caeseele, and P.C. Loewen, Intracellular location of catalase- peroxidase hydroperoxidase I of Escherichia coli. FEMS Microbiol Lett, 1999. 170(2): p. 307-12.
32. Schellhorn, H.E., Regulation of hydroperoxidase (catalase) expression in Escherichia coli. FEMS Microbiology Letters, 1995. 131(2): p. 113-119.
33. Mulvey, M.R., et al., Regulation of transcription of katE and katF in Escherichia coli. J Bacteriol, 1990. 172(12): p. 6713-20.
34. Chiancone, E., et al., Iron and proteins for iron storage and detoxification. Biometals, 2004. 17(3): p. 197-202.
35. Eshelman, K., et al., Inhibiting the BfrB:Bfd interaction in Pseudomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron deficiency in the bacterial cytosol. Metallomics, 2017. 9(6): p. 646-659.
36. Bou-Abdallah, F., et al., Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry. J Biol Chem, 2002. 277(40): p. 37064-9.
37. Ma, J.F., et al., Bacterioferritin A modulates catalase A (KatA) activity and resistance to hydrogen peroxide in Pseudomonas aeruginosa. J Bacteriol, 1999. 181(12): p. 3730-42.
38. Kim, Y.C., C.D. Miller, and A.J. Anderson, Identification of adjacent genes encoding the major catalase and a bacterioferritin from the plant-beneficial bacterium Pseudomonas putida. Gene, 1997. 199(1-2): p. 219-24.
39. Nijkamp, K., et al., The solvent-tolerant Pseudomonas putida S12 as host for the production of cinnamic acid from glucose. Appl Microbiol Biotechnol, 2005. 69(2): p. 170-7.
40. Ishige, T., K. Honda, and S. Shimizu, Whole organism biocatalysis. Curr Opin Chem Biol, 2005. 9(2): p. 174-80.
41. Prather., K.J., 10.492-2 Integrated Chemical Engineering Topics I: Introduction to Biocatalysis. 2004.
42. Hartmans, S., et al., Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X. Appl Environ Microbiol, 1989. 55(11): p. 2850-5.