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• W1874207856 abstract "Yeasts are widely used for the production of heterologous proteins. Improving the expression of such proteins is a top priority for pharmaceutical and industrial applications. N-Glycosylation, a common form of protein modification in yeasts, facilitates proper protein folding and secretion. Accordingly, our previous study revealed that the attachment of additional N-glycans to recombinant elastase by introducing an N-glycosylation sequon at suitable locations could stimulate its expression. Interestingly, the sequon Asn-Xaa-Thr is N-glycosylated more efficiently than Asn-Xaa-Ser, so improving the N-glycosylation efficiency via the conversion of Ser to Thr in the sequon would enhance the efficiency of N-glycosylation and increase glycoprotein expression. Recently, the expression level of recombinant elastase was enhanced by this means in our lab. Actually, the modification of N-glycosylation sites can generally be achieved through site-directed mutagenesis; thus, the method described in this report represents a feasible means of improving heterologous protein expression in yeasts." @default.
• W1874207856 created "2016-06-24" @default.
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• W1874207856 date "2015-02-11" @default.
• W1874207856 modified "2023-10-13" @default.
• W1874207856 title "Enhanced expression of heterologous proteins in yeast cells via the modification of<i>N</i>-glycosylation sites" @default.
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• W1874207856 doi "https://doi.org/10.1080/21655979.2015.1011031" @default.
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