Introduction of an N-Glycosylation Site Increases Secretion of Heterologous Proteins in Yeasts |
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Authors: | C M J Sagt B Kleizen R Verwaal M D M de Jong W H Müller A Smits C Visser J Boonstra A J Verkleij and C T Verrips |
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Institution: | C. M. J. Sagt, B. Kleizen, R. Verwaal, M. D. M. de Jong, W. H. Müller, A. Smits, C. Visser, J. Boonstra, A. J. Verkleij, and C. T. Verrips |
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Abstract: | Saccharomyces cerevisiae is often used to produce heterologous proteins that are preferentially secreted to increase economic feasibility. We used N-glycosylation as a tool to enhance protein secretion. Secretion of cutinase, a lipase, and llama VHH antibody fragments by S. cerevisiae or Pichia pastoris improved following the introduction of an N-glycosylation site. When we introduced an N-glycosylation consensus sequence in the N-terminal region of a hydrophobic cutinase, secretion increased fivefold. If an N-glycosylation site was introduced in the C-terminal region, however, secretion increased only 1.8-fold. These results indicate that the use of N glycosylation can significantly enhance heterologous protein secretion. |
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