Skip to main content
Log in

A hyper-thermostable, alkaline lipase from Pseudomonas sp. with the property of thermal activation

  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

A hyper-thermostable, alkaline lipase from a newly-isolated, mesophilic Pseudomonas sp. was optimal at pH 11 and at 90 °C. It had a half-life of more than 13 h at 90 °C. It was activated by 30% when heated at 90 °C for 2 h. The enzyme had a greater affinity for mustard oil (K m=40 mg ml−1) than for olive oil (K m=140 mg ml−1).

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Ghosh PK, Saxena RK, Gupta R, Yadav RP, Davidson WS (1996) Microbial lipases: production and applications. Sci. Prog. 79: 119–157.

    Google Scholar 

  • Gilbert EJ (1993) Pseudomonas lipases: biochemical properties and molecular cloning. Enzyme Microbiol. Tech. 15: 634–645.

    Google Scholar 

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

    Google Scholar 

  • Klump H, Di-Ruggiero J, Kessel M, Park JB, Adams MWW, Robb FT (1992) Glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. J. Biol. Chem. 267: 22681–22685.

    Google Scholar 

  • Kulkarni N, Gadre RV (1999) A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp. Biotechnol. Lett. 21: 897–899.

    Google Scholar 

  • Lee SY, Rhee JS (1993) Production and partial purification of a lipase from Pseudomonas putida 3SK. Enzyme Microbiol. Tech. 15: 617–623.

    Google Scholar 

  • Nahas E (1988) Control of lipase production by Rhizopus oligosporus under various growth conditions. J. Gen. Microbiol. 134: 227–233.

    Google Scholar 

  • Nawani N, Dosanjh NS, Kaur J (1998) A novel thermostable lipase from a thermophilic Bacillus sp.: characterization and esterification studies. Biotechnol. Lett. 20: 997–1000.

    Google Scholar 

  • Nishio T, Chikano T, Kamimura M (1987) Purification and some properties of lipase produced by Pseudomonas fragi 22.39B. Agric. Biol. Chem. 51: 181–186.

    Google Scholar 

  • Taipa MA, Aires-Barros MR, Cabral JMS (1992) Purification of lipases. J. Biotechnol. 26: 111–142.

    Google Scholar 

  • Vulfson EN (1994) Industrial application of lipases. In: Woolley P, Petersen SB, eds. Lipases: Their Structure, Biochemistry and Application. Cambridge: Cambridge University Press, pp. 271–288.

    Google Scholar 

  • Watanabe N, Ota Y, Minoda Y, Yamada K (1977) Isolation and identification of alkaline lipase producing microorganisms, cultural conditions and some properties of crude enzymes. Agric. Biol. Chem. 41: 1353–1358.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Rathi, P., Bradoo, S., Saxena, R. et al. A hyper-thermostable, alkaline lipase from Pseudomonas sp. with the property of thermal activation. Biotechnology Letters 22, 495–498 (2000). https://doi.org/10.1023/A:1005604617440

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005604617440

Navigation