Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris

  • Published : 2004.02.01
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Abstract

Ferritin is an iron storage protein found in most living organisms. For expression and industrial use, human light chain ferritin (L-ferritin) was cloned from human liver cDNA library and expressed in Pichia pastoris strain GS115. The recombinant L-ferritin in Pichia pastoris was glycosylated. In a fed-batch culture, the cell mass reached about 57 g/l of dry cell weight, and the L-ferritin in the cell was increased to about 95 mg/l after 150 h. In an atomic absorption spectrometry analysis, the intracellular content of iron in the L-ferritin transformant was measured as $1,694{\pm}85\;\mu\textrm{g}g/g$, which is 5.4-fold more than that of the control strain. This L-ferritin transformant could serve as iron-fortified nutrients in animal feed stock.

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