Combining expression and process engineering for high-quality production of human sialyltransferase in Pichia pastoris
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- 作者：Christiane Luley-Goedla ; Tibor Czabanyb ; Karin Longusb ; Katharina Schmö ; lzera ; Sabine Zitzenbachera ; Doris Ribitscha ; Helmut Schwabc ; Bernd Nidetzkya ; b ; bernd.nidetzky@tugraz.at" class="auth_mail" title="E-mail the corresponding author
- 关键词：CMP-Neu5Ac ; cytidine-5&prime ; -monophospho-N-acetylneuraminic acid ; ST6Gal-I ; human β-galactoside α2 ; 6-sialyltransferase I ; YPD-broth ; yeast extract-peptone-glucose/dextrose broth ; YPG-broth ; yeast extract-peptone-glycerol broth
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：10 October 2016
- 年：2016
- 卷：235
- 期：Complete
- 页码：54-60
- 全文大小：861 K
文摘
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The N-terminally truncated variant Δ108 of human sialyltransferase STGal-I was produced in Pichia pastoris.
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Protection of the N-terminal region was important to prevent protein degradation.
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Expression and process engineering were combined to gain 17 units/L of bioreactor culture.
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Mixed glycerol/methanol feed was key for high enzyme titers.
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Enzyme was recovered efficiently using anion exchange chromatography.