Journal of Microbiology and Biotechnology

  • 제28권8호
  • /
  • Pages.1346-1351
  • /
  • 2018
  • /
  • 1017-7825(pISSN)
  • /
  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지
DOI QR코드

DOI QR Code

Cofactor Regeneration Using Permeabilized Escherichia coli Expressing NAD(P)+-Dependent Glycerol-3-Phosphate Dehydrogenase

  • Rho, Ho Sik (Department of Chemical and Material Engineering, The University of Suwon) ;
  • Choi, Kyungoh (Department of Chemical and Material Engineering, The University of Suwon)
  • 투고 : 2018.03.08
  • 심사 : 2018.05.15
  • 발행 : 2018.08.28
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Oxidoreductases are effective biocatalysts, but their practical use is limited by the need for large quantities of NAD(P)H. In this study, a whole-cell biocatalyst for NAD(P)H cofactor regeneration was developed using the economical substrate glycerol. This cofactor regeneration system employs permeabilized Escherichia coli cells in which the glpD and gldA genes were deleted and the gpsA gene, which encodes $NAD(P)^+-dependent$ glycerol-3-phosphate dehydrogenase, was overexpressed. These manipulations were applied to block a side reaction (i.e., the conversion of glycerol to dihydroxyacetone) and to switch the glpD-encoding enzyme reaction to a gpsA-encoding enzyme reaction that generates both NADH and NADPH. We demonstrated the performance of the cofactor regeneration system using a lactate dehydrogenase reaction as a coupling reaction model. The developed biocatalyst involves an economical substrate, bifunctional regeneration of NAD(P)H, and simple reaction conditions as well as a stable environment for enzymes, and is thus applicable to a variety of oxidoreductase reactions requiring NAD(P)H regeneration.

키워드

참고문헌

  1. Uppada V, Bhaduri S, Noronha SB. 2014. Cofactor regeneration; an important aspect of biocatalysis. Curr. Sci. 106: 946-957.
  2. Wang X, Saba T, Yiu HHP, Howe RF, Anderson JA, Shi J. 2017. Cofactor NAD(P)H regeneration inspired by heterogeneous pathways. Chem 2: 621-654. https://doi.org/10.1016/j.chempr.2017.04.009
  3. Stewart JD. 2001. Dehydrogenases and transaminases in asymmetric synthesis. Curr. Opin. Chem. Biol. 5: 120-129. https://doi.org/10.1016/S1367-5931(00)00180-0
  4. Li Z, van Beilen JB, Duetz WA, Schmid A, de Raadt A, Griengl H, et al. 2002. Oxidative biotransformations using oxygenases. Curr. Opin. Chem. Biol. 6: 136-144. https://doi.org/10.1016/S1367-5931(02)00296-X
  5. Hummel W, Kula MR. 1989. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 184: 1-13. https://doi.org/10.1111/j.1432-1033.1989.tb14983.x
  6. van der Donk WA, Zhao H. 2003. Recent developments in pyridine nucleotide regeneration. Curr. Opin. Biotechnol. 14: 421-426. https://doi.org/10.1016/S0958-1669(03)00094-6
  7. Wichmann R, Vasic-Racki D. 2005. Cofactor regeneration at the lab scale. Adv. Biochem. Eng. Biotechnol. 92: 225-260.
  8. Tishkov VI, Popov VO. 2006. Protein engineering of formate dehydrogenase. Biomol. Eng. 23: 89-110. https://doi.org/10.1016/j.bioeng.2006.02.003
  9. Schubert T, Hummel W, Muller M. 2002. Highly enantioselective preparation of multifunctionalized propargylic building blocks. Angew. Chem. Int. Ed. 41: 634-637. https://doi.org/10.1002/1521-3773(20020215)41:4<634::AID-ANIE634>3.0.CO;2-U
  10. Wong C-H, Whitesides GM. 1981. Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and the glucose-5-phosphate dehydrogenase from Leuconostoc mesenteroides. J. Am. Chem. Soc. 103: 4890-4899. https://doi.org/10.1021/ja00406a037
  11. Kataoka M , Sri Rohani L P, Wada M, Kita K, Yanase H , Urabe I, et al. 1998. Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system. Biosci. Biotechnol. Biochem. 62: 167-169. https://doi.org/10.1271/bbb.62.167
  12. Costas AM, White AK, Metcalf WW. 2001. Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88. J. Biol. Chem. 276: 17429-17436. https://doi.org/10.1074/jbc.M011764200
  13. Johannes TW, Woodyer RD, Zhao H. 2007. Efficient regeneration of NADPH using an engineered phosphite dehydrogenase. Biotechnol. Bioeng. 96: 18-26. https://doi.org/10.1002/bit.21168
  14. Choi KO, Song SH, Yoo YJ. 2004. Permeabilization of Ochrobactrum anthropi SY509 cells with organic solvents for whole cell biocatalyst. Biotechnol. Bioproc. Eng. 9: 147-150. https://doi.org/10.1007/BF02942284
  15. Sakasegawa S, Hagemeier CH, Thauer RK, Essen LO, Shima S. 2004. Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference. Protein Sci. 13: 3161-3171.
  16. Rahmat N, Abdullah AZ, Mohamed AR. 2010. Recent progress on innovative and potential technologies for glycerol transformation into fuel additives: a critical review. Renew. Sust. Energy Rev. 14: 987-1000. https://doi.org/10.1016/j.rser.2009.11.010
  17. da Silva GP, Mack M, Contiero J. 2009. Glycerol: a promising and abundant carbon source for industrial microbiology. Biotechnol. Adv. 27: 30-39. https://doi.org/10.1016/j.biotechadv.2008.07.006
  18. Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97: 6640-6645. https://doi.org/10.1073/pnas.120163297
  19. Oguri S, Watanabe K, Nozu A, Kamiya A. 2007. Screening of D-amino acid oxidase inhibitor by a new multi-assay method. Food Chem. 100: 616-622. https://doi.org/10.1016/j.foodchem.2005.09.076

피인용 문헌

  1. Comparative global metabolite profiling of xylose-fermenting Saccharomyces cerevisiae SR8 and Scheffersomyces stipitis vol.103, pp.13, 2019, https://doi.org/10.1007/s00253-019-09829-5
  2. Sustainable biosynthesis of chemicals from methane and glycerol via reconstruction of multi‐carbon utilizing pathway in obligate methanotrophic bacteria vol.14, pp.6, 2018, https://doi.org/10.1111/1751-7915.13809
  3. Kinetic modelling of 2,3-butanediol production by Raoultella terrigena CECT 4519 resting cells: Effect of fluid dynamics conditions and initial glycerol concentration vol.176, pp.None, 2018, https://doi.org/10.1016/j.bej.2021.108185