Food Science and Biotechnology

  • 제18권2호
  • /
  • Pages.494-499
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  • 2009
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  • 1226-7708(pISSN)
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  • 2092-6456(eISSN)
한국식품과학회 (Korean Society of Food Science and Technology)
권호 표지

Enhanced Activity of Phenylalanine Ammonia Lyase in Permeabilised Recombinant E. coli by Response Surface Method

  • Cui, Jian-dong (Hebei Fermentation Engineering Research Center, College of Bioscience and Bioengineering, Hebei University of Science and Technology) ;
  • Li, Yan (Hebei Fermentation Engineering Research Center, College of Bioscience and Bioengineering, Hebei University of Science and Technology) ;
  • Jia, Shi-Ru (Key Laboratory of Industry Microbiology, Ministry of Education, Tianjin University of Science and Technology)
  • 발행 : 2009.04.30
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초록

To improve phenylalanine ammonia lyase (E.C.4.3.1.5-PAL) activity in recombinant Escherichia coli, Some approaches for improving phenylalanine ammonia lyase (PAL) activity in recombinant E. coli were developed following preliminary studies by means of response surface method. The results shown that permeabilization with combination of Triton X-100, cetyl trimethyl ammonium bromide (CTAB), and acetone enriched cellular recombinant PAL activity significantly, which improved over 10-fold as compared with the control (untreat cell), as high as 181.37 U/g. The optimum values for the tested variables were Triton X-100 0.108 g/L, CTAB 0.15 g/L, and acetone 45.2%(v/v). Furthermore, a second-order model equation was suggested and then validated experimentally. It was indicated that addition of surfactants and organic solvents made the cells more permeable and therefore allowed easier access of the substrate to the enzyme and excretion of the product, which increased the rate of transport of L-phenylalanine and trans-cinnamic acids. These improved methods of PAL activity enrichment could serve as a rich enzyme source, especially in the biosynthesis of L-phenylalanine.

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참고문헌

  1. Fiske MJ, Kane JF. Regulation of phenylalanine biosynthesis in Rhodotorula glutinis. J. Bacteriol. 160: 676-681 (1984)
  2. Rosler J, Krekel F, Amrhein N. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol. 113: 175-179 (1997) https://doi.org/10.1104/pp.113.1.175
  3. Nakamichi K, Yamada NS, Chibata I. Induction and stabilization of L-phenylalanine ammonia lyase activity in Rhodotorula glutinis. Eur. J. Appl. Microbiol. 18: 158-162 (1983) https://doi.org/10.1007/BF00498038
  4. Srinivasan AR, Nagajyothi R, Gowda LR. Phenylalanine ammonia lyase activity enhancement in permeabilized yeast cells (Rhodotorula glutinis). Biotechniques 8: 729-732 (1994)
  5. D'Cunha GB. Enrichment of phenylalanine ammonia lyase activity of Rhosotorula yeast. Enzyme. Microb. Technol. 36: 498-502 (2005) https://doi.org/10.1016/j.enzmictec.2004.11.006
  6. Orum H, Rasmussen OF. Expression in E. coli of the gene encoding phenylalanine ammonia lyase from Rhodosporidium toruloides. Appl. Microbiol. Biot. 36: 745-748 (1992)
  7. Faulkner JDB, Anson JG, Tuite MF. High-level expression of the phenylalanine ammonia lyase-encoding gene from Rhodosporidium toruloides in Sacchpromyces cerevisiae and Escherichia coli using a bifunctional expression system. Gene 143: 13-20 (1994) https://doi.org/10.1016/0378-1119(94)90598-3
  8. Avishek M, Arun G. Enhanced prodution of exocellular glucansucrase from Leuconostoc dextranicum NRRL B-1146 using response surface methodology. Bioresource Technol. 99: 3685-3691 (2008) https://doi.org/10.1016/j.biortech.2007.07.027
  9. Liyana-Pathirana C, Shahidi F. Optimization of extraction of phenolic compounds from wheat using surface response methodology. Food. Chem. 9: 347-356 (2005)
  10. Cui JD, Jia SR, Sun AY. Influence of amino acids, organic solvents, and surfactants for phenylalanine ammonia lyase activity in recombinant E. coli. Lett. Appl. Microbiol. 46: 631-635 (2008) https://doi.org/10.1111/j.1472-765X.2008.02364.x
  11. Jia SR, Cui JD, Li Y. Production of L-phenylalanine from transcinnamic acids by high-level expression of phenylalanine ammonia lyase gene from Rhodosporidium toruloides in Escherichia coli. Biochem. Eng. J. 42: 193-197 (2008) https://doi.org/10.1016/j.bej.2008.06.010
  12. Delisa MP, Rao G, Weigand WA. Monitoring GFP-operon fusion protein expression during high cell density cultivation of Escherichia coli using an on-line optical sensor. Biotechnol. Bioeng. 65: 54-64 (1999) https://doi.org/10.1002/(SICI)1097-0290(19991005)65:1<54::AID-BIT7>3.0.CO;2-R
  13. Paik H-D, Kim I-G, Lee J-H, Park K-Y, Ji G-E, Jin T-E, Rhim S-L. Heterologous expression of α-amylase gene of Bifidobacterium adolescentis Int57 in Bacillus polyfermenticus SCD. Food Sci. Biotechnol. 16: 655-658 (2007)
  14. Orndorff SA, Costantino N, Stewart D. Strain improvement of Rhodotorula graminis for production of a novel L-phenylalanine ammonia-lyase. Appl. Environ. Microb. 54: 996-1002 (1988)
  15. Song JY, Keum I-K, Jin Q, Park J-M, Kim BS, Jung BH, Kim T-J, Han NS. Batch and fed-batch production of hyperthermostable $\alpha$-Larabinofuranosidase of Thermotoga maritima in recombinant E. coli by using constitutive and inducible promoters. Food Sci. Biotechnol. 17: 990-995 (2008)
  16. Yuan Q, Yue H. PAL activity and productivity of L-phenylalanine in the production of L-phenylalanine. J. Beijing. Univ. Chem. Technol. China 30: 1-3 (2003)
  17. Myers RH, Montgomery DC. Response Surface Methodology:Process and Product Optimization Using Designed Experiments. 2nd ed. John Wiley and Sons, New York, NY, USA. pp. 146-149 (2002)
  18. Jung SJ, Jang MS. Effects of wasabi stalk on the fermentation of baechukimchi. Food Sci. Biotechnol. 17: 692-699 (2008)
  19. EI-Batal AI. Optimization of reation conditions and stabilization of phenylalanine ammonia lyase-containing Rhosotorula glutinis cells during bioconversion of trans-cinnamic acid to L-phenylalanine. Acta Microbiol. Pol. 51: 139-152 (2002)
  20. Wang QH, Ma H, Xu W, Gong L, Zhang W, Zou D. Ethanol production from kitchen garbage using response surface methodology. Biochem. Eng. J. 39: 604-610 (2008) https://doi.org/10.1016/j.bej.2007.12.018
  21. Oskouie SFG, Fatemeh T, Bagher Y, Fereshteh E. Response surface optimization of medium composion for alkaline protease production by Bacillus clausii. Biochem. Eng. J. 39: 37-42 (2008) https://doi.org/10.1016/j.bej.2007.08.016