ArticleApplied microbiology and biotechnology2025
Expression of functional human sialyltransferases ST6GalNAc5 and ST6GalNAc6 in Pichia pastoris.
Article in Applied microbiology and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The two sialyltransferases in the ST6GALNAC subfamily (EC 2.4.99.-; CAZy family GT29), ST6GalNAc5 and ST6GalNAc6, catalyze the formation of the linkage from the sialic acid moiety to the C6 position of N-acetylgalactosamine (GalNAc) as well as to N-acetylglucosamine (GlcNAc), and are known as α-2,6-sialyltransferases. This activity is interesting for the synthesis of the disialylated oligosaccharide disialyllacto-N-tetraose (DSLNT). Human sialyltransferases ST6GalNAc5 and ST6GalNAc6 produced in HEK293 cells are commercially available at a smaller scale. In this study, we demonstrated that ST6GalNAc5 and ST6GalNAc6 can be functionally expressed in Pichia pastoris X-33. The level of ST6GalNAc5 and ST6GalNAc6 expression and activity largely depended on the type of construct, as well as on expression conditions, namely temperature, methanol feeding regime, and supplements. Insertion of a (GGGS)₂ linker peptide between the gene and the α secretion factor improved the secretion of active enzyme in P. pastoris X-33. The use of media supplemented with MgCl
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