Production, characterization, and application of an organic solvent-tolerant lipase present in active inclusion bodies

Applied Biochemistry and Biotechnology

Volumn 169, Issue 2, 2013, Pages 612-623

  Li, Suxia ^a   Lin, Kang ^a   Pang, Huaiyu ^a   Wu, Yixin ^b   Xu, Jianhe ^a  

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

^b HAMAMATSU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

( ) MPGM; Active inclusion body; Lipase; Organic solvent tolerance; Serratia marcescens ECU1010

Indexed keywords

ACTIVATION MECHANISMS; ACTIVITY ASSAYS; AFTER-TREATMENT; BIOTECHNOLOGICAL APPLICATIONS; CULTURE BROTHS; ENZYMATIC ACTIVITIES; FOURIER TRANSFORM INFRARED MICROSPECTROSCOPY; GLYCIDIC ACIDS; HIGH CONCENTRATION; HIGH-CELL-DENSITY CULTIVATIONS; INCLUSION BODIES; ISOPROPYL ETHERS; KINETIC RESOLUTION; LIPASE ACTIVITY; METHYL ESTERS; ORGANIC SOLVENT TOLERANCE; ORGANIC SOLVENT-TOLERANT LIPASE; ORGANIC SYNTHESIS; PH VALUE; PHARMACEUTICAL INDUSTRY; SERRATIA MARCESCENS; WET WEIGHT;

CELL CULTURE; ESCHERICHIA COLI; ETHERS; LIPASES; MICROOPTICS; ORGANIC COMPOUNDS; SCANNING ELECTRON MICROSCOPY;

ORGANIC SOLVENTS;

3 (4 METHOXYPHENYL)GLYCIDIC ACID METHYL ESTER; BACTERIAL ENZYME; DIISOPROPYL ETHER; ORGANIC SOLVENT; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ARTICLE; BIOMASS PRODUCTION; CELL DENSITY; CELL INCLUSION; CONTROLLED STUDY; ENANTIOSELECTIVITY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; MICROBIAL BIOMASS; NONHUMAN; PH; PROTEIN EXPRESSION; SCANNING ELECTRON MICROSCOPY; SERRATIA MARCESCENS; TEMPERATURE;

ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; INCLUSION BODIES; LIPASE; ORGANIC CHEMICALS; PROTEIN ENGINEERING; SERRATIA MARCESCENS; SOLVENTS;

ESCHERICHIA COLI; SERRATIA MARCESCENS;

EID: 84873082463     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-012-0028-7     Document Type: Article

References (39)

1. Keasling, J. D. (2008). Synthetic biology for synthetic chemistry. ACS Chemical Biology, 3, 64-76.
2. Jong, H.C.; Ki, C.K.; Sang, Y.L. (2006) Production of recombinant proteins by high cell density culture of Escherichia coli. Chemical Engineering Science, 61, 876-885.
3. Ami, D.; Natalello, A.; Taylor, G.; Tonon, G.; & Doglia, S. M. (2006). Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochimica et Biophysica Acta, 1764, 793-799.
4. Gonzalez-Montalban, N.; García-Fruitós, E.; Ventura, S.; Aris, A.; & Villaverde, A. (2006). The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microbial Cell Factories, 5, 26.
5. Arie, J. P.; Miot, M.; Sassoon, N.; & Betton, J. M. (2006). Formation of active inclusion bodies in the periplasm of Escherichia coli. Molecular Microbiology, 62, 427-437.
6. García-Fruitós, E.; González-Montalbán, N.; Morell, M.; Vera, A.; Ferraz, R. M.; Arís, A.; et al. (2005). Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microbial Cell Factories, 4, 27.
7. Indu, B.; Rajinder, P.; Gulam, N. Q.; et al. (2008). Lipase enzyme immobilization on synthetic beaded macroporous copolymers for kinetic resolution of chiral drugs intermediates. Process Biochemistry, 43, 321-330.
8. Gandhi, N. N. (1997). Applications of lipase. Journal of the American Oil Chemists' Society, 74, 621-634.
9. Ribeiro, C. M. R.; Passaroto, E. N.; & Brenelli, E. C. S. (2001). Enzymatic resolution of ethyl 3-hydroxy-3-phenylpropanoate and analogs using hydrolases. Journal of the Brazilian Chemical Society, 12, 742-746.
10. Frings, K.; Koch, M.; & Hartmeier, W. (1999). Kinetic resolution of 1-phenyl ethanol with high enantioselectivity with native and immobilized lipase in organic solvents. Enzyme and Microbial Technology, 25, 303-309.
11. Ying-Yang, J.; Martin, S.; & Hans-Ulrich, B. (2002). The enantioselective hydrogenation of 1-phenyl ethanol and of ketones using Pt and Pd supported on natural polymers. Journal of Molecular Catalysis A: Chemical, 177, 307-308.
12. Singh, S.; & Banerjee, U. C. (2007). Purification and characterization of trans-3-(4-methoxyphenyl) glycidic acid methyl ester hydrolyzing lipase from Pseudomonas aeruginosa. Process Biochemistry, 42, 1063-1068.
13. Nagao, T.; Sato, M.; Nakajima, H.; & Kiyomoto, A. (1972). Studies on a new 1,5-benzothiazapine derivative (CRD-401). II. Vasodilator actions. Japanese Journal of Pharmacology, 22, 1-10.
14. Hulshof, L.A.; Roskan, J.H. (1989) Phenylglycidate stereoisomers, conversion products thereof with e.g. 2-nitrothiophenol and preparation of diltiazem. European Patent Application 343714.
15. Matsumae, H.; Furui, M.; & Shibatani, T. (1993). Lipase-catalyzed asymmetric hydrolysis of 3-phenylglycidic acid ester, the key intermediate in synthesis of Diltiazem hydrochloride. Journal of Fermentation and Bioengineering, 75, 93-98.
16. Long, Z. D.; Xu, J. H.; Zhao, L. L.; Pan, J.; Yang, S.; & Hua, L. (2007). Overexpression of Serratia marcescens lipase in Escherichia coli for efficient bioresolution of racemic ketoprofen. Journal of Molecular Catalysis B: Enzymatic, 47, 105-110.
17. Gao, L.; Xu, J. H.; & Li, X. J. (2004). Optimization of Serratia marcescens lipase production for enantioselective hydrolysis of 3-phenyl glycidic acid ester. Journal Industry Microbiology Biotechnology, 31, 525-530.
18. Chin, J. H.; Rahman, R. N. Z. A.; Salleh, A. B.; & Basri, M. (2003). A newly isolated organic solvent-tolerant Bacillus sphaericus 205y producing organic solvent-stable lipase. Biochemical Engineering Journal, 15, 147-151.
19. Diletta, A.; Antonino, N.; Pietro, G. L.; Marina, L.; & Silvia, M. D. (2005). Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Letters, 579, 3433-3436.
20. Lee, S. Y. (1996). High cell-density culture of Escherichia coli. Trends in Biotechnology, 14, 98-105.
21. Seo, D. J.; Chung, B. H.; Hwang, Y. B.; & Park, Y. H. (1992). Glucose-limited fed-batch culture of Escherichia coli for production of recombinant human interleukin-2 with the DO-Stat method. Journal of Fermentation and Bioengineering, 74, 196-198.
22. Gupta, R.; Gupta, N.; & Rathi, P. (2004). Bacterial lipases: An overview of production, purification and biochemical properties. Applied Microbiology and Biotechnology, 64, 763-781.
23. Yuzo, K.; Michihiko, K.; & Sakayu, S. (2003). A novel lipase from Pseudomonas fluorescens HU380: Gene cloning, overproduction, renaturation-activation, two-step purification, and characterization. Journal of Bioscience and Bioengineering, 96, 242-249.
24. Zhang, A. J.; Gao, R. J.; Diao, N. B.; Xie, G. Q.; et al. (2009). Cloning, expression and characterization of an organic solvent tolerant lipase from Pseudomonas fluorescens JCM5963. Journal of Molecular Catalysis B: Enzymatic, 56, 78-84.
25. Akatsuka, H.; Kawai, E.; Omori, K.; Komatsubara, S.; Shibatani, T.; & Tosa, T. (1994). The lipA gene of Serratia marcescens which encodes an extracellular lipase having no N-terminal signal peptide. Journal of Bacteriology, 176, 1949-1956.
26. Amada, K.; Haruki, M.; Imanaka, T.; Morikawa, M.; & Kanaya, S. (2000). Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38. Biochimica et Biophysica Acta, 1478, 201-210.
27. Rollof, J.; Hedstrom, S. A.; & Nilsson-Ehle, P. (1987). Positional specificity and substrate preference of purified Staphylococcus aureus lipase. Biochimica et Biophysica Acta, 921, 370-377.
28. Zhao, L. L.; Xu, J. H.; Zhao, J.; Pan, J.; & Wang, Z. L. (2008). Biochemical properties and potential applications of an organic solvent tolerant lipase isolated from Serratia marcescens ECU1010. Process Biochemistry, 43, 626-633.
29. Shibatani, T.; Matsumae, H.; Akatsuka, H. (1991) Esterase from Serratia and process for preparing the same. European Patent Application 446771.
30. Salamone, P. R.; & Wodzinski, R. J. (1997). Production, purification and characterization of a 50-kDa extracellular metalloprotease from Serratia marcescens. Applied Microbiology and Biotechnology, 48, 317-324.
31. Li, S. X.; Pang, H. Y.; Lin, K.; Xu, J. H.; et al. (2011). Refolding, purification and characterization of an organic solvent-tolerant lipase from Serratia marcescens ECU1010. Journal of Molecular Catalysis B: Enzymatic, 71, 171-176.
32. Henley, J. P.; & Sadana, A. (1985). Categorization of enzyme deactivations using a series-type mechanism. Enzyme and Microbial Technology, 7, 50-60.
33. Kojima, Y.; Yokoe, M.; & Mase, T. (1994). Purification and characterization of an alkaline lipase from Pseudomonas fluorescens AK102. Bioscience, Biotechnology, and Biochemistry, 58, 1564-1568.
34. Matsumae, H.; & Shibatani, T. (1994). Purification and characterization of the lipase from Serratia marcescens Sr41 8000 responsible for asymmetric hydrolysis of 3-phenylglycidic acid esters. Journal of Bioscience and Bioengineering, 77, 152-158.
35. Schmidt-Dannert, C.; Sztajer, H.; Stocklein, W.; Menge, U.; & Schmid, R. D. (1994). Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochimica et Biophysica Acta, 1214, 43-53.
36. Klibanov, A. M. (1997). Why are enzymes less active in organic solvents than in water?. Trends in Biotechnology, 15, 97-101.
37. Zaks, A.; & Klibanov, A. M. (1988). Enzymatic catalysis in nonaqueous solvents. Journal of Biological Chemistry, 263, 3194-3201.
38. Carrió, M. M.; Corchero, J. L.; & Villaverde, A. (1998). Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria. FEMS Microbiology Letters, 169, 9-15.
39. Przybycien, T. M.; Dunn, J. P.; Valax, P.; & Georgiou, G. (1994). Secondary structure characterization of beta-lactamase inclusion bodies. Protein Engineering, 7, 131-136.