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A novel esterase Sso2518 from Sulfolobus solfataricus with a much lower temperature optimum than the growth temperature

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An Erratum to this article was published on 13 May 2010

Abstract

An esterase, Sso2518, from Sulfolobus solfataricus P2 was over-expressed in E. coli. and characterized after purification. The maximum activity was at pH 7.5 and 50°C. The half life of Sso2518 was about 30 min at 85°C and the enzyme was activated by Cu2+. The catalytic triad of Sso2518 was comprised of residues Ser151, Asp176, and His328. Sso2518 showed the highest activity with p-nitrophenyl caproate (C6) and could also hydrolyze olive oil. Under native conditions, Sso2518 consists of 125 kDa homotrimers.

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References

  • Abramic M, Lescic I, Korica T (1999) Purification and properties of extracellular lipase from Streptomyces rimosus. Enzyme Microb Technol 25:522–529

    Article  CAS  Google Scholar 

  • Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410

    CAS  PubMed  Google Scholar 

  • Bryant P, Kriek M, Wood RJ, Roach PL (2006) The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate. Anal Biochem 351:44–49

    Article  CAS  PubMed  Google Scholar 

  • Cacciapuoti G, Porcelli M, De Rosa M, Gambacorta A, Bertoldo C, Zappia V (1991) S-adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus. Purification, molecular properties and studies on the covalently bound pyruvate. Eur J Biochem 199:395–400

    Article  CAS  PubMed  Google Scholar 

  • Ding Y, Cai Y, Zhang G, Xu W (2004) The influence of dipeptide composition on protein thermostability. FEBS Lett 569:284–288

    Article  CAS  PubMed  Google Scholar 

  • Fisher CL, Pei GK (1997) Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23:570–574

    CAS  PubMed  Google Scholar 

  • Han D, Krauss G (2009) Characterization of the endonuclease SSO2001 from Sulfolobus solfataricus P2. FEBS Lett 583:771–776

    Article  CAS  PubMed  Google Scholar 

  • Jaeger KE, Ransac S, Dijkstra BW, Colson C, van Heuvel M, Misset O (1994) Bacterial lipases. FEMS Microbiol 15:29–63

    Article  CAS  Google Scholar 

  • Kim S, Lee SB (2004) Thermostable esterase from a thermoacidophilic archaeon: purification and characterization for enzymatic resolution of a chiral compound. Biosci Biotechnol Biochem 68:2289–2298

    Article  CAS  PubMed  Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Article  CAS  PubMed  Google Scholar 

  • Merone L, Mandrich L, Rossi M, Manco G (2005) A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles 9:297–305

    Article  CAS  PubMed  Google Scholar 

  • Milo RE, Duffner FM, Müller R (1999) Catechol 2, 3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability. Extremophiles 3:185–190

    Article  CAS  PubMed  Google Scholar 

  • Park Y, Choi SY, Lee HB (2006) A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression. Biochim Biophys Acta 1760:820–828

    CAS  PubMed  Google Scholar 

  • She Q, Singh RK, Confalonieri F et al (2001) The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc Natl Acad Sci 98:7835–7840

    Article  CAS  PubMed  Google Scholar 

  • Suzuki Y, Miyamoto K, Ohta H (2004) A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7. FEMS Microbiol Lett 236:97–102

    Article  CAS  PubMed  Google Scholar 

  • Talker-Huiber D, Jose J, Glieder A, Pressnig M, Stubenrauch G, Schwab H (2003) Esterase EstE from Xanthomonas vesicatoria (Xv_EstE) is an outer membrane protein capable of hydrolyzing long-chain polar esters. Appl Microbiol Biotechnol 61:479–487

    CAS  PubMed  Google Scholar 

  • Wang J, Cao Y, Zheng G (2009) Mutation in the RGD motif decreases the esterase activity of Xcc_est. Biotechnol Lett 31:1445–1449

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgement

This work was supported by Youth Fund of State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences and Open fund of State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences.

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Authors and Affiliations

  1. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, People’s Republic of China

    Jianjun Wang

  2. State Key Laboratory of Chemical Resources Engineering, Beijing University of Chemical Technology, Beijing, 100029, People’s Republic of China

    Jiayi Wang, Xiangyu Gong & Guojun Zheng

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  1. Jianjun Wang
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  2. Jiayi Wang
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  3. Xiangyu Gong
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  4. Guojun Zheng
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Corresponding author

Correspondence to Guojun Zheng.

Additional information

Jiayi Wang shared the first author.

An erratum to this article can be found at http://dx.doi.org/10.1007/s10529-010-0299-4

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Wang, J., Wang, J., Gong, X. et al. A novel esterase Sso2518 from Sulfolobus solfataricus with a much lower temperature optimum than the growth temperature. Biotechnol Lett 32, 1103–1108 (2010). https://doi.org/10.1007/s10529-010-0261-5

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  • DOI: https://doi.org/10.1007/s10529-010-0261-5

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