Culture conditions affect the category and production of ubiquinones in a recombinant escherichia coli with an exogenous decaprenyl diphosphate synthase

被引:0
作者
Li, Jiazhou [1 ,2 ]
Zhang, Yuanyuan [2 ]
Xie, Mingquan [1 ]
Luo, Xiaochun [1 ]
机构
[1] School of Bioscience and Bioengineer, South China University of Technology
[2] Department of Food and Bioengineering, Guangdong Industry Technical College
来源
Luo, X. | 1600年 / Maxwell Science Publications, 74, Kenelm Road,, B10, 9AJ, Birmingham, Small Heath, United Kingdom卷 / 05期
关键词
Decaprenyl diphosphate synthase; Escherichia coli; Rhizobium radiobacter; Ubiquinone;
D O I
10.19026/ajfst.5.3080
中图分类号
学科分类号
摘要
Ubiquinones (UQ) are important electron transporters and play lot of important roles in most organisms. In different species, UQ was classified to be UQ-6, 7, 8, 9, 10 according to their polyprenyl side chain length. The side chain's length is determined by the enzyme named Poly-Prenyl diphosphate Synthases (PPPS). Bacteria are usually reconstructed to producing UQ-10 used in human's food additive, medicine or cosmetics, such as using decaprenyl Diphosphate Synthase (DPS) gene from R. radiobacter to substitute E. coli's octaprenyl diphosphate synthase gene, just like E. coli BL21 (ΔispB::ddsA) used in this study. It is interesting that not only in these reconstructed bacteria, but in human-being, DPS can synthesize UQ-9 besides UQ-10. The mechanism of this phenomenon is still unknown. In this study, the effects of culture conditions, including the temperature, dissolved oxygen, pH and culture medium, on the DPS characteristics in E. coli BL21 (ΔispB::ddsA) were examined. Results show that temperature greatly affects the ratio of UQ-9/UQ-10, but not the total ubiquinone's production. Increasing dissolved oxygen and protein concentration in culture medium can promote total ubiquinone's production, but not the ratio of UQ-9/UQ-10. These results may give reference for UQ-10's industrial produce and the mechanism of these conditions' effect on DPS will be discussed.
引用
收藏
页码:1186 / 1191
页数:5
相关论文
共 38 条
  • [1] Aberg F., Appelkvist E.L., Dallner G., Ernster L., Distribution and redox state of ubiquinones in rat and human tissues, Arch. Biochem. Biophys., 295, pp. 230-234, (1992)
  • [2] Bader M.W., Xie T., Yu C.A., Bardwell J.C., Disulfide bonds are generated by quinone reduction, J. Biol. Chem., 275, pp. 26082-26088, (2000)
  • [3] Battino M., Ferri E., Gorini A., Villa R.F., Rodriguez Huertas J.F., Fiorella P., Genova M.L., Lenaz G., Marchetti M., Natural distribution and occurrence of coenzyme Q homologues, Membr. Biochem., 9, pp. 179-190, (1990)
  • [4] Bhataya A., Schmidt-Dannert C., Lee P.C., Metabolic engineering of Pichia pastoris X-33 for lycopene production, Process. Biochem., 44, pp. 1095-1102, (2009)
  • [5] Brandt U., Trumpower B., The protonmotive Q cycle in mitochondria and bacteria, Crit. Rev. Biochem. Mol. Biol., 29, pp. 165-197, (1994)
  • [6] Chang H.T., Guo R.T., Ko T.P., Wang A.H., Liang P.H., Crystal of structure-III geranylgeranyl pyrophosphate synthase from Saccharomyces cerevisiae and the mechanism of product chain length determination, J. Biol. Chem., 281, pp. 14991-15000, (2006)
  • [7] Clarke C.F., New advance in coenzyme Q biosynthesis, Protoplasma, 213, pp. 134-147, (2000)
  • [8] Datsenko K.A., Wanner B.L., One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products, Proc. Natl. Acad. Sci. USA, 97, pp. 6640-6645, (2000)
  • [9] Echtay K.S., Winkler E., Frischmuth K., Klingenberg M., Uncoupling proteins 2 and 3 are highly active H(+) transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone), Proc. Natl. Acad. Sci. USA, 98, pp. 1416-1421, (2001)
  • [10] Gomez-Diaz C., Rodriguez-Aguilera J.C., Barroso M.P., Villalba J.M., Navarro F., Crane F.L., Navas P., Antioxidant ascorbate is stabilized by NADH-coenzyme Q(10) reductase in the plasma membrane, J. Bioenerg. Biomembr., 29, pp. 251-257, (1997)