Cellular and Molecular Life Sciences

, Volume 64, Issue 21, pp 2841–2847 | Cite as

A cold-active salmon goose-type lysozyme with high heat tolerance

  • P. Kyomuhendo
  • B. Myrnes
  • I. W. NilsenEmail author
Research Article


The Atlantic salmon (Salmo salar) goose-type lysozyme gene was isolated and revealed alternative splicing within exon 2 affecting the signal peptide-encoding region. The lysozyme was produced in Escherichia coli, and the recombinant enzyme showed a high specific lytic activity that was stimulated by low or moderate concentrations of mono- or divalent cations. Relative lytic activities of 70 and 100% were measured at 4°C and 22°C, respectively, and there was no detectable activity at 60°C. However, 30% activity was retained after heating the enzyme for 3 h at 90°C. This unique combination of thermal properties was surprising since the salmon goose-type lysozyme contains no cysteines for protein structure stabilization through disulphide bond formation. The results point to a rapid reversal of inactivation, probably due to instant protein refolding.


Atlantic salmon immunity lysozyme goose-type gene protein cold-active thermal tolerance 


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Copyright information

© Birkhaueser 2007

Authors and Affiliations

  1. 1.Marine Biotechnology and Fish HealthNorwegian Institute of Fisheries & AquacultureTromsøNorway

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