Optimized condition for enhanced soluble-expression of recombinant mutant Anabaena variabilis phenylalanine ammonia lyase

Advanced Pharmaceutical Bulletin

Volumn 4, Issue 3, 2014, Pages 261-266

  Jaliani, Hossein Zarei ^a,b   Farajnia, Safar ^a,c   Safdari, Yaghoub ^c   Mohammadi, Seyyed Abolghasem ^d   Barzegar, Abolfazl ^d   Talebi, Saeed ^e  

^a TABRIZ UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b TABRIZ UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^c TABRIZ UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^d UNIVERSITY OF TABRIZ   (Iran)

^e AVICENNA RESEARCH INSTITUTE   (Iran)

Author keywords

Optimization; Phenylalanine ammonia lyase; Soluble expression; Specific activity

Indexed keywords

PHENYLALANINE AMMONIA LYASE; RECOMBINANT PROTEIN;

ANABAENA VARIABILIS; ARTICLE; BACTERIUM MUTANT; CONCENTRATION (PARAMETERS); ENZYME ACTIVITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENETIC CODE; NONHUMAN; PROCESS OPTIMIZATION; PROTEIN EXPRESSION;

EID: 84983579907     PISSN: 22285881     EISSN: 22517308     Source Type: Journal    
DOI: 10.5681/apb.2014.038     Document Type: Article

References (21)

1. Blau N, Van Spronsen FJ, Levy HL. Phenylketonuria. Lancet 2010;376(9750):1417-27.
2. Kim W, Erlandsen H, Surendran S, Stevens RC, Gamez A, Michols-Matalon K, et al. Trends in enzyme therapy for phenylketonuria. Mol Ther 2004;10(2):220-4.
3. Moffitt MC, Louie GV, Bowman ME, Pence J, Noel JP, Moore BS. Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization. Biochemistry 2007;46(4):1004-12.
4. Wang L, Gamez A, Archer H, Abola EE, Sarkissian CN, Fitzpatrick P, et al. Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase. J Mol Biol 2008;380(4):623-35.
5. Sahdev S, Khattar SK, Saini KS. Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Mol Cell Biochem 2008;307(1-2):249-64.
6. Lilie H, Schwarz E, Rudolph R. Advances in refolding of proteins produced in E. coli. Curr Opin Biotechnol 1998;9(5):497-501.
7. Moazen F, Rastegari A, Hoseini SM, Panjehpour M, Miroliaei M, Sadeghi HM. Optimization of Taq DNA polymerase enzyme expression in Escherichia coli. Adv Biomed Res 2012;1:82.
8. Rezaei M, Zarkesh-Esfahani SH. Optimization of production of recombinant human growth hormone in Escherichia coli. J Res Med Sci 2012;17(7):681-5.
9. Sadeghi HM, Rabbani M, Rismani E, Moazen F, Khodabakhsh F, Dormiani K, et al. Optimization of the expression of reteplase in Escherichia coli. Res Pharm Sci 2011;6(2):87-92.
10. Sengupta P, Meena K, Mukherjee R, Jain SK, Maithal K. Optimized conditions for high-level expression and purification of recombinant human interleukin-2 in E. coli. Indian J Biochem Biophys 2008;45(2):91-7.
11. Jaliani HZ, Farajnia S, Mohammadi SA, Barzegar A, Talebi S. Engineering and kinetic stabilization of the therapeutic enzyme Anabeana variabilis phenylalanine ammonia lyase. Appl Biochem Biotechnol 2013;171(7):1805-18.
12. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
13. Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat Methods 2012;9(7):671-5.
14. Baedeker M, Schulz GE. Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase. Structure 2002;10(1):61-7.
15. Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry 2004;43(36):11403-16.
16. Ritter H, Schulz GE. Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase. Plant Cell 2004;16(12):3426-36.
17. Li RY, Cheng CY. Investigation of inclusion body formation in recombinant Escherichia coli with a bioimaging system. J Biosci Bioeng 2009;107(5):512-5.
18. Vera A, Gonzalez-Montalban N, Aris A, Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol Bioeng 2007;96(6):1101-6.
19. Cirkovas A, Sereikaite J. Increase in the solubility of the recombinant mink growth hormone at low cultivation temperature of E. coli. Biotechnol Biotec Eq 2010;24(4):2169-71.
20. Tripathi NK, Shrivastva A, Biswal KC, Rao PV. Optimization of culture medium for production of recombinant dengue protein in Escherichia coli. Ind Biotechnol 2009;5(3):179-83.
21. Hartinger D, Heinl S, Schwartz HE, Grabherr R, Schatzmayr G, Haltrich D, et al. Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B(1). Microb Cell Fact 2010;9:62.