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Factors affecting the acyltransfer activity of the lipase fromCandida parapsilosis in aqueous media

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Journal of the American Oil Chemists’ Society

Abstract

This study describes the influence of various factors on the hydrolysis and alcoholysis activities of the lipase fromCandida parapsilosis (Ashford), Langeron and Talice in aqueous media. Optimal activities were obtained at 45°C and pH 6–6.5. The influence of the nature of the substrate on the temperature activity profiles was observed. Total or partial recovery of the activities was obtained when methanol was added to the enzyme extract after thermal denaturation. A tyrosin residue appeared to be necessary for lipase function. Magnesium was a required metal cofactor. These activities were optimal in the presence of high amounts of water (water activity >0.9).

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References

  1. Riaublanc, A., R. Ratomahenina, P. Galzy and M. Nicolas, Peculiar Properties of Lipase fromCandida parapsilosis (Ashford) Langeron and Talice,JAOCS 70:497–500 (1993).

    CAS  Google Scholar 

  2. Briand, D., E. Dubreucq and P. Galzy, Enzymatic Fatty Esters Synthesis in Aqueous Medium with Lipase fromCandida parapsilosis (Ashford) Langeron and Talice,Biotechnol. Lett. 16:813–818 (1994).

    Article  CAS  Google Scholar 

  3. Galzy, P., Etude Génétique et Physiologique du Métabolisme de L’acide Lactique ChezSaccharomyces cerevisiae HANSEN,Ann. Technol. Agric. 13:109–259 (1964).

    Google Scholar 

  4. Biehn, G.F., and M.L. Ernsberger, Polyvinyl Alcohol as an Emulsifying Agent,Ind. Eng. Chem. 40:1449–1453 (1948).

    Article  CAS  Google Scholar 

  5. Van Autryve, P., R. Ratomahenina, A. Riaublanc, C. Mitrani, J. Graille and P. Galzy, Spectrophotoemetry Assay of Lipase Activity Using Rhodamine 6G,Oléagineux 46:29–31 (1991).

    Google Scholar 

  6. Faber, K., and S. Riva, Enzyme-Catalysed Irreversible Acyl Transfer,Synthesis:895–910 (1992).

  7. Nakatani, T., J. Hiratake, K. Yoshikawa, T. Nishioka and J. Oda, Chemical Inactivation of Lipase in Organic Solvent: A Lipase fromPseudomonas aeruginosa TE3285 Is More Like a Typical Serine Enzyme in an Organic Solvent Than in Aqueous Media,Biosci. Biotech. Biochem. 56:1118–1123 (1992).

    Article  CAS  Google Scholar 

  8. Malcata, F.X., H.R. Reyes, H.S. Garcia, C.G. Hill, Jr. and C.H. Amundson, Kinetics and Mechanisms of Reactions Catalysed by Immobilised Lipases,Enzyme Microb. Technol. 14:426–444 (1992).

    Article  CAS  Google Scholar 

  9. Brockerhoff, H., and R.G. Jensen, Kinetics of Lipolysis and Lipases, inLipolytic Enzymes, Academic Press, Inc., London, 1974, pp. 18–28.

    Google Scholar 

  10. Penasse, L., Le Centre Actif inLes Enzymes: Cinétique et Mécanisme D’action, edited by Masson et Cie, Paris, 1974, pp. 82–114.

  11. Hirs, C.H.W., Cleavage of Peptide Chains, inMethods in Enzymology, edited by S.P. Colowick and N.O. Kaplan, Academic Press, New York and London, 1967, pp. 21–322.

    Google Scholar 

  12. Philipis, J.L., and D. Azari, Modification of Carboxylic Groups in Enzymes,Biochem 10:1160 (1971).

    Article  Google Scholar 

  13. Bourgois, A., M. Fourgeron and C. de Preval, For the Determination of Tryptophan in Proteins,Eur. J. Biochem. 24:446–455 (1972).

    Article  CAS  Google Scholar 

  14. Macrae, A.R., and R.C. Hammond, Present and Future Applications of Lipases,Biotechnol. Gen. Bioeng. Rev. 3:193–217 (1985).

    CAS  Google Scholar 

  15. Penasse, L., Thermodynamique Enzymatique inLes Enzymes: Cinétique et Mécanisme D’action, edited by Masson et Cie, Paris, 1974, pp. 115–144.

  16. Goldberg, M., D. Thomas and M.D. Legoy, The Control of Lipase-Catalysed Transesterification and Esterification Reaction Rates, Effects of Substrate Polarity, Water Activity and Water Molecules on Enzyme Activity,Eur. J. Biochem. 190:603–609 (1990).

    Article  CAS  Google Scholar 

  17. Valivety, R.H., P.J. Halling, A.D. Peilow and A.R. Macrae, Lipases from Different Sources Vary Widely in Dependence of Catalytic Activity on Water Activity,Biochim. Biophys. Acta 1122:143–146 (1992).

    CAS  Google Scholar 

  18. Monot, F., E. Paccard, F. Borzeix, M. Bardin and J.P. Vandecasteele, Effect of Lipase Conditioning on Its Activity in Organic Media,Appl. Microbiol. Biotechnol. 39:483–486 (1993).

    Article  CAS  Google Scholar 

  19. Deutscher, M.P., Maintaining Protein Stability inMethods in Enzymology, edited by M.P. Deutscher, Academic Press, Inc., London, 1990, pp. 83–89.

    Google Scholar 

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Authors and Affiliations

  1. ENSA.M-INRA, Laboratoire de Microbiologie Industrielle et de Génétique des Microorganismes, 2 Place Viala, 34060, Montpellier Cedex 1, France

    Delphine Briand, Eric Dubreucq & Pierre Galzy

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  1. Delphine Briand
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  2. Eric Dubreucq
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  3. Pierre Galzy
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Briand, D., Dubreucq, E. & Galzy, P. Factors affecting the acyltransfer activity of the lipase fromCandida parapsilosis in aqueous media. J Am Oil Chem Soc 72, 1367–1373 (1995). https://doi.org/10.1007/BF02546213

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  • DOI: https://doi.org/10.1007/BF02546213

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