Abstract

The biotechnological relevance of protein glycosylation has exponentially grown in recent years. With the advances in protein glycosylation research, new possibilities for glyco-engineering have arisen, and a wide array of glycans can be designed and potentially transferred to target proteins in the biotechnologically relevant host Escherichia coli. Here we provide insight on how to select the best strains and plasmids. We also describe methods for determination of glycan expression and assembly, protein glycosylation using western blot, and preparation of samples for mass spectrometry.

Original languageEnglish
Pages (from-to)57-70
Number of pages14
JournalMethods in molecular biology (Clifton, N.J.)
Volume1321
DOIs
StatePublished - Jan 1 2015

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