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- W3150014568 abstract "N-glycosylation is one of the most important posttranslational modification of proteins in eukaryotes.A rational strategy to introduce N-glycosylation site was proposed to Armillariella tabescens beta mannose Man47.Then g-123 mutant with EAS(enhanced aromatic sequence) sequence was built through the molecular docking,secondary structure analysis and feasibility analysis of glycosylation.The sequence of g-123mutant was inserted into SMD1168 with the yeast α-mating factor,then transformed it into Piclua by electroporation to obtain the recombinants.Finally the thermal stability,acid and alkali stability,pepsinresistance and trypsin-resistance of g-123 and wild type were analyzed.The results showed that compared with wild type,the thermal stability,acid and alkali stability,protease resistance of the mutant g-123 with glycosylation was improved." @default.
- W3150014568 created "2021-04-13" @default.
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- W3150014568 date "2013-01-01" @default.
- W3150014568 modified "2023-09-25" @default.
- W3150014568 title "The Stability Reconstruction of β-mannanase with N-glycosylation Modification" @default.
- W3150014568 hasPublicationYear "2013" @default.
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