Log in

Determination of amino acids and dipeptides is correlated significantly with optimum temperatures of microbial lipases

  • Original Article
  • Published:
Annals of Microbiology Aims and scope Submit manuscript

Abstract

Amino acids and dipeptides that are correlated significantly with lipase optimum temperatures were searched for in 34 microbial lipase sequences by a stepwise regression method. The positive dipeptides were found to be IR, KS, NY, SA, ST and YR, whereas negative ones were DK, DY, IS, KA, WS, YS and QI. The calculated optimum temperatures from an optimal regression equation of dipeptides fitted the corresponding experimental optimum temperatures of lipases very well, and the maximal absolute difference was only 3.43°C. The spatial positions of the related dipeptides were searched for in two known crystal structures of a thermophilic and mesophilic lipase, respectively. Most of the positive dipeptides were sited in the α-helices, while the negative ones were located mainly in the β-strands or coils and about half of them existed in the N- or C-terminii of the lipases. The results obtained will be very useful in lipase engineering for enhancing lipase thermostability.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price includes VAT (Thailand)

Instant access to the full article PDF.

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM (2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. J Mol Biol 341:1271–1281

    Article  PubMed  CAS  Google Scholar 

  • Akoh CC, Lee GC, Shaw JF (2004) Protein engineering and applications of Candida rugosa lipase isoforms. Lipids 39:513–526

    Article  PubMed  CAS  Google Scholar 

  • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181:223–230

    Article  PubMed  CAS  Google Scholar 

  • Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson GG, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343:767–770

    Article  PubMed  CAS  Google Scholar 

  • Chakravarty S, Varadarajan R (2000) Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett 470:65–69

    Article  PubMed  CAS  Google Scholar 

  • Cote A, Shareck F (2008) Cloning, purification and characterization of two lipases from Streptomyces coelicolor A3. Enzyme Microb Technol 42:381–388

    Article  CAS  Google Scholar 

  • Declerck N, Machius M, Wiegand G, Hube R, Gaillardin C (2000) Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase. J Mol Biol 301:1041–1057

    Article  PubMed  CAS  Google Scholar 

  • Ding YR, Cai YJ, Zhang GX, Xu WB (2004) The influence of dipeptide composition on protein thermostability. FEBS Lett 569:284–288

    Article  PubMed  CAS  Google Scholar 

  • Gatti-Lafranconi P, Caldarazzo SM, Villa A, Alberghina L, Lotti M (2008) Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase. FEBS Lett 582:2313–2318

    Article  PubMed  CAS  Google Scholar 

  • Han ZL, Han SY, Zheng SP, Lin Y (2009) Enhancing thermostability of a Rhizomucor miehei lipase by engineering a disulfide bond and displaying on the yeast cell surface. Appl Microbiol Biotechnol 85:117–126

    Article  PubMed  CAS  Google Scholar 

  • Karplus PA, Schulz GE (1985) Prediction of chain flexibility in proteins, a tool of the selection of peptide antigens. Naturwissenschaften 72:212–213

    Article  CAS  Google Scholar 

  • Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S (2002) Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 13A resolution. Acta Crystallogr, Sect D: Biol Crystallogr 58:1168–1174

    Article  Google Scholar 

  • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409:241–245

    Article  PubMed  CAS  Google Scholar 

  • Li WF, Zhou XX, Lu P (2005) Structural features of thermozymes. Biotechnol Adv 23:271–281

    Article  PubMed  CAS  Google Scholar 

  • Nelofer R, Ramanan RN, Rahman RNZRA, Basri M, Ariff AB (2011) Sequential optimization of production of a thermostable and organic solvent tolerant lipase by recombinant Escherichia coli. Ann Microbiol 61:535–544

    Article  CAS  Google Scholar 

  • Pack SP, Yoo YJ (2004) Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins. J Biotechnol 111:269–277

    Article  PubMed  CAS  Google Scholar 

  • Panasik JN, Brenchley JE, Farber GK (2000) Distributions of structural features contributing to thermostability in mesophilic and thermophilic α/β barrel glycosyl hydrolases. Biochim Biophy Acta 1543:189–201

    Article  CAS  Google Scholar 

  • Reddy BVB, Ramesh P, Tiwari S (1998) MEICPS: substitution mutations to engineer intracellular protein stability. Bioinformatics 14:225–226

    Article  PubMed  CAS  Google Scholar 

  • Sayari A, Frikha F, Miled N, Mtibaa H, Alia YB, Verger R, Gargouri Y (2005) N-terminal peptide of Rhizopus oryzae lipase is important for its catalytic properties. FEBS Lett 579:976–982

    Article  PubMed  CAS  Google Scholar 

  • Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A (1997) The open conformation of a Pseudomonas lipase. Structure 5:187–202

    Article  PubMed  CAS  Google Scholar 

  • Sharma R, Soni SK, Vohra RM, Gupta LK, Gupta JK (2002) Purification and characterization of a thermostable alkaline lipase from a new thermophilic Bacillus sp RSJ-1. Process Biochem 37:1075–1084

    Article  CAS  Google Scholar 

  • Shi BH, Wu WB, Wen JX, Shi QQ, Wu SG (2010) Cloning and expression of a lipase gene from Bacillus subtilis FS1403 in Escherichia coli. Ann Microbiol 60:399–404

    Article  CAS  Google Scholar 

  • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1–43

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by a grant from The National Natural Science Foundation of China (No. 20776061). We are grateful to Prof. Weida Huang (Department of Biochemistry, School of life Sciences, Fudan University) for providing technical assistance.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Min-Chen Wu.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Zhang, HM., Li, JF., Wu, MC. et al. Determination of amino acids and dipeptides is correlated significantly with optimum temperatures of microbial lipases. Ann Microbiol 63, 307–313 (2013). https://doi.org/10.1007/s13213-012-0475-y

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s13213-012-0475-y

Keywords

Navigation