Effects of induction starting time and Ca2+ on expression of active penicillin G acylase in Escherichia coli

Biotechnology Progress

Volumn 23, Issue 5, 2007, Pages 1031-1037

  Yong, Mei Jiang ^a,b   Wang, Yu Tong ^a   Dong, Zhi Wei ^a  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b Fujian Nomal University   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; CELL GROWTH; ENZYMES; ESCHERICHIA COLI; FERMENTATION;

CELL DENSITY; PENICILLIN G ACYLASE; RECOMBINATION PROTEIN; VOLUMETRIC ACTIVITY;

GENE EXPRESSION;

CALCIUM; PENICILLIN AMIDASE; RECOMBINANT PROTEIN;

ARTICLE; BIOREACTOR; BIOSYNTHESIS; CULTURE TECHNIQUE; DOSE RESPONSE; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; KLUYVERA; METABOLISM; METHODOLOGY; MICROBIOLOGY; PHYSIOLOGY; PROTEIN ENGINEERING; TIME;

BIOREACTORS; CALCIUM; CELL CULTURE TECHNIQUES; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; KLUYVERA; PENICILLIN AMIDASE; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; TIME FACTORS;

ESCHERICHIA COLI; KLUYVERA CRYOCRESCENS;

EID: 35348818686     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070100+     Document Type: Article

References (40)

1. Woestenenk, E. A.; Hammarstrom, M.; Berg, S.; Hard, T.; Berglund, H. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J. Struct. Funct. Genomics 2004, 5, 217-229.
2. Hansen, T; Schlichting, B.; Schonheit, P. Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme. FEMS Microbiol. Lett. 2002, 216, 249-253.
3. Baneyx, F.; Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399-1408.
4. Hammarstrom, M.; Hellgren, N.; van den Berg, S.; Berglund, H.; Torleif, H. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 2002, 11, 313-321.
5. Tresaugues, L.; Collinet, B.; Minard, P. Refolding strategies from inclusion bodies in a structural genomics project. J. Struct. Funct. Genomics 2004, 5, 195-204.
6. Ghosh, S.; Rasheedi, S.; Rahim, S. S. Method for enhancing solubility of the expressed recombinant proteins in Escherichia coli. Biotechniques 2004, 37, 418, 420, 422-423.
7. Machida, S.; Yong, Y.; Satya, P. S.; Jong-Deog, K.; Kiyoshi, H.; Yasushi, K. Overproduction of beta-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. FEMS Microbiol. Lett. 1998, 159, 41-46.
8. Stevens, R. C. Design of high-throughput methods of protein production for structural biology. Structure 2000, 8, 177-185.
9. Clark, E. D. B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 1998, 9, 157-163.
10. Loewe, L.; Textor, V.; Scherer, S. High deleterious genomic mutation rate in stationary phase of Escherichia coli. Science 2003, 302, 1558-1560.
11. Ou, J. x. L. W.; Ding, X. L.; Du, J. Y.; Zhang, Y.; Chen, H. P.; Xu, A. L. Stationary phase protein overproduction is a fundamental capability of Escherichia coli. Biochem. Biophys. Res. Commun. 2004, 314, 174-180.
12. Shewale, J. G.; Deshpande, B. S.; Sudhakaran, V. K.; Ambedkar, S. S. Penicillin acylases: applications and potentials. Process Biochem. 1990, 25, 97-103.
13. Cheng. T. F.; Chen, M. L.; Zheng, H. B. et al. Expression and purifcation of penicillin G acylase enzymes from four diferent microorganisms, and a comparative evaluation of their synthesis/hydrolysis ratios for cephalexin. Protein Expression Purif. 2006, 46 (1), 107-113 MAR.
14. Alvaro, G.; Fernandez-Lafuente, R.; Rosell, C. M.; Blanco, R. M.; Garcia-Lopez, J. L.; Guisan, J. M. Penicillin G acylase from Kluyvera citrohila: new choice as industrial enzyme. Biotechnol. Lett. 1992, 14, 285-290.
15. Bock, A.; Wirth, R.; Schmidt, G.; Schumacher, G.; Lang, G; Buckel, P. The two subunits of penicillin acylase are processed from a common precursor. FEMS Microbiol. Lett. 1983, 20, 141-144.
16. Vojtisek, V.; Slezak, J. Penicillin amidohydrolase in Escherichia coli. III. Catabolite repression, diauxie, effect of cAMP and nature of the enzyme induction. Folia. Microbiol. (Prague) 1975, 20, 298-306.
17. Ignatova, Z.; Hornle, C.; Nurk, A.; Kasche, V. Unusual signal peptide directs penicillin amidase from E. coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 2002, 291, 146-149.
18. 2+-binding: Implications for Folding and Maturation of Ntn-hydrolase Penicillin Amidase from E. coli. J. Mol. Biol. 2005, 348, 999-1014.
19. 2+ is required for transport and maturation and is yield determining factor in high cell density fermentations of penicillin amidase. Biotechnol. Prog. 2005, 21, 432-438.
20. Chou, C. P.; Lin, W. J.; Kuo, B. Y.; Yu, C. C. Genetic strategies to enhance penicillin acylase production in Escherichia coli. Enzyme Microb. Technol. 2000, 27, 766-773.
21. Keilmann, C.; Wanner, G.; Bock, A. Molecular basis of the exclusive low-temperature synthesis of an enzyme in E. coli: penicillin acylase. Biol. Chem. Hoppe-Seyler 1993, 374, 983-992.
22. Merino, E.; Balbas, P.; Recillas, F.; Becerril, B.; Valle, F; Bolivar, F. Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene. Mol. Microbiol. 1992, 6, 2175-2182.
23. Yang, S. L.; Wu, R. P.; Wang, J. X.; He, J. S; Zhang, S. B. Cloning and expression of the penicillin acylase gene. III. Temperature regulates the expression of the penicillin acylase gene at transcriptional level. Chin. J. Biotechnol. 1988, 4, 32-37.
24. Jiang, Q. L.; Wu, R. P; Yang, S. L. Regulatory mode of pac gene expression. Chin. J. Biotechnol. 1992, 8, 213-217.
25. Ignatova, Z.; Mahsunah, A.; Georgieva, M.; Kasche, V. Improvement of posttranslational bottlenecks in the production of penicillin amidase in recombinant Escherichia coli strains. Appl. Environ. Microbiol. 2003, 69, 1237-1245.
26. Lin, W. J.; Huang. S. W.; Chou, C. P. DegP-coexpression minimizes inclusion-body formation upon overproduction of recombinant penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 2001, 73, 484-492.
27. Fu, X. Y.; Tong, W. Y.; Wei, D. Z. Extracellular production of human parathyroid hormone as a thioredoxin fusion form in Escherichia coli by chemical permeabilization combined with heat treatment. Biotechnol. Prog. 2005, 21 (5), 1429-1435.
28. Rodrigues, M.; Guereca, L.; Valle, F.; Quintero, R.; Lopez-Munguia, A. Penicillin acylase extraction by osmotic shock. Process Biochem. 1992, 27, 217-223.
29. Gang, D. M.; Shaikh, K. Regulation of penicillin acylase in Escherichia coli by cyclic AMP. Biochim. Biophys. Acta 1976, 425, 110-114.
30. Schagger, H.; von Jagow, G. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166 (2), 368-379.
31. Galloway, C. A.; Sowden, M. P.; Smith, H. C. Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase. Biotechniques 2003, 34 (3), 524-530.
32. Ignatova, Z.; Enfors, S. O.; Hobbie, M.; Taruttis, S.; Vogt, C.; Kasche V. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli. Enzyme Microb. Technol. 2000, 26, 165-170.
33. Liu, Y. C.; Liao L. C.; Wu, W. T. Cultivation of recombinant Escherichia coli to achieve high cell density with a high level of penicillin G acylase activity. Proc. Natl. Sci. Counc. Repub. China Part B 2000, 24, 156-160.
34. Sobotkova, L.; Stepanek, V.; Plhackova, A.; Kyslik, P. Development of a high-expression system for penicillin G acylase based on the recombinant Escherichia coli strain RE3 (pKA18). Enzyme Microb. Technol. 1996, 19, 389-397.
35. Norris, V.; Grant S.; Freestone, P.; Canvin, J.; Sheikh, N. F.; Toth, I.; Trinei, M.; Modha, K.; Norman, R. I. Ca signalling in bacteria. J. Bacteriol. 1996, 178, 3677-3682.
36. Smith, R. J. Ca and bacteria. Adv. Microb. Physiol. 1995, 37, 83-103.
37. Hewitt, L.; Kasche, V.; Lummer, K.; Lewist, R. J.; Murshudov, G. N.; Verma, G. N. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active cleft. J. Mol. Biol. 2000, 302, 887-898.
38. Duggleby, H. J.; Tolley, S. P.; Hill, C. P.; Dodson, E. J.; Dodson, G. G; Moody, C. E. Penicillin acylase has a single-amino-acid catalytic centre. Nature 1995, 373, 264-268.
39. Hewitt, L.; Kasche, V.; Lummer, K.; Lewist, R. J.; Murshudov, G. N.; Verma, G. N; Dodson, G. G.; Wilson, K. S. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active cleft. J. Mol. Biol. 2000, 302, 887-898.
40. Kasche, V.; Lummer, K.; Nurk, A.; Piotraschke, E.; Rieks, A.; Stoeva, S.; Voelter, W. Intramolecular proteolysis initiates the maturation of penicillin amidase from Escherichia coli. Biochim. Biophys. Acta 1999, 1433, 76-86.