Biochemical and molecular characterisation of Tetrahymena thermophila extracellular cysteine proteasesReportar como inadecuado

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BMC Microbiology

, 6:19

First Online: 28 February 2006Received: 07 October 2005Accepted: 28 February 2006


BackgroundOver the last decades molecular biologic techniques have been developed to alter the genome and proteome of Tetrahymena thermophila thereby providing the basis for recombinant protein expression including functional human enzymes. The biotechnological potential of Tetrahymena has been proved in numerous publications, demonstrating fast growth, high biomass, fermentation in ordinary bacterial-yeast equipment, up-scalability, existence of cheap and chemical defined media. For these reasons Tetrahymena offers promising opportunities for the development of a high expression system. Yet optimised high yield strains with protease deficiency such as commonly used in yeast and bacterial systems are not available.

ResultsThis work presents the molecular identification of predominant proteases secreted into the medium by Tetrahymena thermophila. A one-step purification of the proteolytic enzymes is described.

ConclusionThe information provided will allow silencing of protease activity by either knock out methods or by Tetrahymena specific antisense-ribosome-techniques. This will facilitate the next step in the advancement of this exciting organism for recombinant protein production.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-6-19 contains supplementary material, which is available to authorized users.

Lutz Herrmann, Michael Erkelenz contributed equally to this work.

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Autor: Lutz Herrmann - Michael Erkelenz - Ingo Aldag - Arno Tiedtke - Marcus WW Hartmann


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