High-level expression of non-glycosylated and active staphylokinase from Pichia pastoris.

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ID: 60022
2009
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Abstract
Staphylokinase (SAK) is a promising thrombolytic agent for treating blood-clotting disorders. Recombinant SAK (rSAK) was produced after integration of the gene into Pichia pastoris genome. The recombinant Pichia carrying multiple insertions of the SAK gene yielded high-level (approximately 1 g/l) of extracellular glycosylated rSAK (approximately 18 kDa) with negligible plasminogen activation activity. Addition of tunicamycin during the induction phase resulted in expression of non-glycosylated and highly active rSAK (approximately 15 kDa) from the same clone. Two simple steps of ion-exchange chromatography produced an homogenous rSAK of >95% purity which suitable for future structural and functional studies.
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Authors Apte-Deshpnade, Anjali;Mandal, Goutam;Soorapaneni, Sudheerbabu;Prasad, Bhaskarjyoti;Kumar, Jitendra;Padmanabhan, Sriram;
Journal biotechnology letters
Year 2009
DOI 10.1007/s10529-009-9938-z
URL
Keywords
pichia pastoris high-level expression methanol codon optimization staphylokinase specific activity

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