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A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp.

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Abstract

An extracellular, alkali-tolerant, thermostable lipase was from a Pseudomonas sp. It had optimal activity at 65 °C and retained 75% of its activity at 65 °C for 90 min. The pH optimum was 9.6 and it retained more than 70% activity between pH 5 and 9 for 2 h. The culture broth was free of protease and, at 30 °C, the culture filtrate retained all the activity for at least 7 days, without any stabilizer. In shake flask culture, addition of groundnut oil (3 g l−1) towards the end of growth phase increased the activity from 4 U ml−1 to 8 ml−1.

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References

  • Berto P, Belingheri L, Dehorter B (1997) Production and purification of a novel extracellular lipase from Alterneria brassicola. Biotechnol. Lett. 19: 533–536.

    Google Scholar 

  • Castellar MR, Taipa MA, Cabral JMS (1997) Kinetic and stability characterization of Chromobacterium viscosum lipase and its comparison with Pseudomonas glumae lipase. Appl. Biochem. Biotechnol. 61: 299–314.

    Google Scholar 

  • Cordenons A, Gonzalez R, Kok R, Hellingwerf KJ, Nudel C (1996) Effect of nitrogen sources on the regulation of extracellular lipase production in Acinetobacter calcoaceticus strains. Biotechnol. Lett. 18: 633–638.

    Google Scholar 

  • Dharmsthiti S, Kuhasuntisuk B (1998) Lipase from Pseudomonas aeruginosa LP602: biochemical properties and application for wastewater treatment. J. Ind. Microbiol. Biotechnol. 21: 75–80.

    Google Scholar 

  • Gilbert EJ, Cornish A, Jones CW (1991) Purification and properties of extracellular lipase from Pseudomonas aeruginosa EF2. J. Gen. Microbiol. 137: 2223–2229.

    Google Scholar 

  • Kojima Y, Yokoe M, Mase T (1994) Purification and characterization of an alkaline lipase from Pseudomonas fluorescens AK102. Biosci. Biotechnol. Biochem. 58: 1564–1568.

    Google Scholar 

  • Kulkarni N, Gadre RV (1998) Simple gas chromatography method for lipase assay. Biotechnol. Tech. 12: 627–628.

    Google Scholar 

  • Kumura H, Mikawa K, Saito Z (1991) Effect of protease on concomitant lipase produced by Pseudomonas sp. No. 33. Milchwissenschaft 46: 215–218.

    Google Scholar 

  • Kunitz M (1947) Crystalline soybean trypsin inhibitor. J. Gen. Physiol. 30: 291–310.

    Google Scholar 

  • Lin SF (1996) Production and stabilization of a solvent-tolerant alkaline lipase from Pseudomonas pseudoalcaligens. J. Ferm. Bioeng. 82: 448–451.

    Google Scholar 

  • Palleroni NJ (1984) Family Pseudomonadaceae. In: Krieg NR, Holt JG, eds. Bergey's Manual of Systematic Bacteriology, Vol. 1. Baltimore: Williams & Wilkins, pp. 141–199.

    Google Scholar 

  • Tan KH, Gill CO (1985) Effect of culture conditions on batch growth of Pseudomonas fluorescens on olive oil. Appl. Microbiol. Biotechnol. 23: 27–32.

    Google Scholar 

  • Winkler UK, Stuckmann M (1979) Glycogen, hyluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J. Bacteriol. 138: 663–670.

    Google Scholar 

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Kulkarni, N., Gadre, R. A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp.. Biotechnology Letters 21, 897–899 (1999). https://doi.org/10.1023/A:1005591009596

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  • DOI: https://doi.org/10.1023/A:1005591009596

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