Please use this identifier to cite or link to this item: http://hdl.handle.net/1946/13288
The aim of this research project was to produce recombinant cod trypsin I in two different cold-adapted protein expression systems, Escherichia coli and Pseudoalteromonas haloplanktis. The results show that the P. haloplanktis system is better suited for expression of the recombinant trypsin I than the E. coli system. The specific activity of the recombinant cod trypsin I was 39.8 U/mg in the P. haloplanktis expression system compared to 17.9 U/mg in previous expression experiments. For comparison, the specific activity of the native cod trypsin I is 63.1 U/mg. The total trypsin activity obtained per volume is higher in the P. haloplanktis protein expression system than previously observed using other expression systems. Cod offal remains an important resource for trypsins but the recombinant trypsin I may be better suited to meet pharmaceutical standards and can provide a stable complimentary source of trypsin I. The findings of this study are important for scaling up the production of cod trypsin I.
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