Production and characterization of two N-terminal truncated esterases from Thermus thermophilus HB27 in a mesophilic yeast: Effect of N-terminus in thermal activity and stability

Protein Expression and Purification

Volumn 78, Issue 2, 2011, Pages 120-130

  Fuciños, Pablo ^a   Atanes, Estrella ^a   López López, Olalla ^b   Esperanza Cerdan M ^b   Isabel Gonzalez Siso M ^b   Pastrana, Lorenzo ^a   Luisa Rua M ^a  

^a UNIVERSITY OF VIGO   (Spain)

^b UNIVERSITY OF A CORUÑA   (Spain)

Author keywords

Heterologous expression; N terminally truncated esterase; Thermal stability; Thermophilic esterase; Thermus thermophilus

Indexed keywords

4 NITROPHENOL; 4-NITROPHENOL; ESTERASE; HYBRID PROTEIN; NITROPHENOL;

AMINO ACID SEQUENCE; ANALYSIS OF VARIANCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; ENZYMOLOGY; GLYCOSYLATION; ISOLATION AND PURIFICATION; KLUYVEROMYCES; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PH; PROTEIN PROCESSING; PROTEIN STABILITY; TEMPERATURE; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; ANALYSIS OF VARIANCE; CLONING, MOLECULAR; ESTERASES; GLYCOSYLATION; HYDROGEN-ION CONCENTRATION; KLUYVEROMYCES; MOLECULAR SEQUENCE DATA; NITROPHENOLS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; TEMPERATURE; THERMUS THERMOPHILUS;

KLUYVEROMYCES LACTIS; THERMUS THERMOPHILUS;

EID: 79958765624     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.04.002     Document Type: Article

References (37)

1. U.T. Bornscheuer, Microbial carboxyl esterases: classification, properties and application in biocatalysis, FEMS Microbiol. Rev. 26 (2002) 73-81. (Pubitemid 34454776)
2. T. Panda, B.S. Gowrishankar, Production and applications of esterases, Appl. Microbiol. Biotechnol. 67 (2005) 160-169. (Pubitemid 40598020)
3. M. Konarzycka-Bessler, K.E. Jaeger, Select the best: novel biocatalysts for industrial applications, Trends Biotechnol. 24 (2006) 248-250. (Pubitemid 43831240)
4. G. Antranikian, Thermophiles: biology and technology at high temperatures, in: F. Robb, G. Antranikian, D. Grogan, A. Driessen (Eds.), Industrial Relevance of Thermophiles and Their Enzymes, CRC Press, Boca Raton, Florida, 2008, pp. 113-160.
5. F. Deive, M. Costas, M. Longo, Production of a thermostable extracellular lipase by Kluyveromyces marxianus, Biotechnol. Lett. 25 (2003) 1403-1406.
6. P. Fuciños, C.M. Abadín, A. Sanromán, M.A. Longo, L. Pastrana, M.L. Rúa, Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: partial purification and preliminary biochemical characterisation, J. Biotechnol. 117 (2005) 233-241.
7. P. Fuciños, A. Domínguez, M. Sanromán, M. Longo, M. Rúa, L. Pastrana, Production of thermostable lipolytic activity by Thermus species, Biotechnol. Prog. 21 (2005) 1198-1205.
8. P. Fuciños, L. Pastrana, A. Sanromán, M.A. Longo, J. Hermoso, M.L. Rúa, An esterase from Thermus thermophilus HB27 with hyper-thermoalkalophilic properties: purification, characterisation and structural modelling. J. Mol. Cat. B Enzym. (2011). doi:10.1016/j.molcatb.2011. 02.017.
9. O. López-López, P. Fuciños, L. Pastrana, M. Rúa, M. Cerdán, M. González-Siso, Heterologous expression of an esterase from Thermus thermophilus HB27 in Saccharomyces cerevisiae, J. Biotechnol. 145 (2010) 226-232.
10. J.D. Bendtsen, H. Nielsen, G. Von Heijne, S. Brunak, Improved prediction of signal peptides: SignalP 3.0, J. Mol. Biol. 340 (2004) 783-795.
11. Y. Kashino, Separation methods in the analysis of protein membrane complexes, J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 797 (2003) 191-216. (Pubitemid 37421306)
12. M. Mueller, R. Takemasa, A. Schwarz, H. Atomi, B. Nidetzky, "Short-chain" [alpha]-1,4-glucan phosphorylase having a truncated N-terminal domain: functional expression and characterization of the enzyme from Sulfolobus solfataricus, BBA-Proteins Proteomics 1794 (2009) 1709-1714.
13. H. Sakuraba, H. Tsuge, I. Shimoya, R. Kawakami, S. Goda, Y. Kawarabayasi, N. Katunuma, H. Ago, M. Miyano, T. Ohshima, The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5- phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix, J. Biol. Chem. 278 (2003) 10799-10806. (Pubitemid 36800353)
14. Y. Suzuki, K. Takano, S. Kanaya, Stabilities and activities of the N- and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli, FEBS J. 272 (2005) 632-642. (Pubitemid 40208868)
15. N. Marianayagam, M. Sunde, J. Matthews, The power of two: protein dimerization in biology, Trends Biochem. Sci. 29 (2004) 618-625.
16. C. Vieille, G.J. Zeikus, Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability, Microbiol. Mol. Biol. Rev. 65 (2001) 1-43.
17. J. Byun, J. Rhee, D. Kim, J. Oh, H. Cho, Crystallization and preliminary X-ray crystallographic analysis of EstE1, a new and thermostable esterase cloned from a metagenomic library, Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 145-147.
18. D. Marchuk, M. Drumm, A. Saulino, F. Collins, Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products, Nucleic Acids Res. 19 (1991) 1154.
19. S.L. Akhnazarova, V.V. Kafarov, Experiment optimization in chemistry and chemical Engineering, revised ed., MIR Publishers, Moscow, 1982.
20. G.E.P. Box, J.S. Hunter, W.G. Hunter, Statistics for Experimenters: Design, Innovation, and Discovery, 2nd ed., John Wiley & Sons Inc., Hoboken, New Jersey, 2005.
21. P. Fuciños, M. Rúa, M. Longo, M. Sanromán, L. Pastrana, Thermal spring water enhances lipolytic activity in Thermus thermophilus HB27, Process Biochem. 43 (2008) 1383-1390.
22. M.L. Rúa, C. Schmidt-Dannert, S. Wahl, A. Sprauer, R.D. Schmid, Thermoalkalophilic lipase of Bacillus thermocatenulatus large-scale production, purification and properties: aggregation behaviour and its effect on activity, J. Biotechnol. 56 (1997) 89-102. (Pubitemid 27391877)
23. A.J. van Ooyen, P. Dekker, M. Huang, M.M. Olsthoorn, D.I. Jacobs, P.A. Colussi, C.H. Taron, Heterologous protein production in the yeast Kluyveromyces lactis, FEMS Yeast Res. 6 (2006) 381-392.
24. P. Qasba, Involvement of sugars in protein-protein interactions, Carbohydr. Polym. 41 (2000) 293-309.
25. J. Cheleski, R.F. Freitas, H.J. Wiggers, J.R. Rocha, A.P. de Araújo, C.A. Montanari, Expression, purification and kinetic characterization of His-tagged glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi, Protein Expr. Purif. 76 (2011) 190-196.
26. C. Aragon, S. Ferreira-Dias, E. de Lucca Gattás, M. de Freitas Sanches Peres, Characterization of glycerol kinase from baker's yeast: Response surface modeling of the enzymatic reaction, J. Mol. Cat. B Enzym. 52-53 (2008) 113-120.
27. Y. Hung, C. Peng, J. Tzen, M. Chen, J. Liu, Immobilization of Neocallimastix patriciarum xylanase on artificial oil bodies and statistical optimization of enzyme activity, Bioresour. Technol. 99 (2008) 8662-8666.
28. Z. Mayerhoff, I. Roberto, T. Franco, Response surface methodology as an approach to determine the optimal activities of xylose reductase and xylitol dehydrogenase enzymes from Candida Mogii, Appl. Microbiol. Biotechnol. 70 (2006) 761-767. (Pubitemid 43772205)
29. M.D. Benaiges, M. Alarcón, P. Fuciños, P. Ferrer, M. Rua, F. Valero, Recombinant Candida rugosa lipase 2 from Pichia pastoris: Immobilization and use as biocatalyst in a stereoselective reaction, Biotechnol. Prog. 26 (2010) 1252-1258.
30. N. López, M. Pernas, L. Pastrana, A. Sánchez, F. Valero, M. Rúa, Reactivity of pure Candida rugosa lipase isoenzymes (Lip1, Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media, Biotechnol. Prog. 20 (2004) 65-73.
31. L. Mandrich, L. Merone, M. Pezzullo, L. Cipolla, F. Nicotra, M. Rossi, G. Manco, Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family, J. Mol. Biol. 345 (2005) 501-512. (Pubitemid 39575920)
32. C. Peña-Montes, S. Lange, D. Castro-Ochoa, K. Ruiz-Noria, F. Cruz-García, R. Schmid, A. Navarro-Ocaña, A. Farrés, Differences in biocatalytic behavior between two variants of StcI esterase from Aspergillus nidulans and its potential use in biocatalysis, J. Mol. Cat. B Enzym. 61 (2009) 225-234.
33. Z. Zhang, B. Zheng, Y. Wang, Y. Chen, G. Manco, Y. Feng, The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity, Biochim. Biophys. Acta 1784 (2008) 1176-1183.
34. F. Foglia, L. Mandrich, M. Pezzullo, G. Graziano, G. Barone, M. Rossi, G. Manco, P. Del Vecchio, Role of the N-terminal region for the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius, Biophys. Chem. 127 (2007) 113-122.
35. E.M. du Plessis, E. Berger, T. Stark, M.E. Louw, D. Visser, Characterization of a novel thermostable esterase from Thermus scotoductus SA-01: evidence of a new family of lipolytic esterases, Current Microbiology 60 (2010) 248-253.
36. H. Sanderová, H. Tiserová, I. Barvík, L. Sojka, J. Jonák, L. Krásný, The N-terminal region is crucial for the thermostability of the G-domain of Bacillus stearothermophilus EF-Tu, Biochim. Biophys. Acta 1804 (2010) 147-155.
37. N. Li, P. Shi, P. Yang, Y. Wang, H. Luo, Y. Bai, Z. Zhou, B. Yao, A xylanase with high pH stability from Streptomyces sp. S27 and its carbohydrate-binding module with/without linker-region-truncated versions, Appl. Microbiol. Biotechnol. 83 (2009) 99-107.