Abstract
The methylotropic yeast Pichia pastoris has been extensively used in large-scale production of properly folded recombinant proteins. As an eukaryotic organism P. pastoris presents a series of advantages at expression and processing of heterologous proteins such as post-translational modifications, protein processing, and a reasonably sophisticated quality control of protein folding when compared against Escherichia coli. In this chapter, we describe the modified lab procedure for cloning and expression in Pichia pastoris of common food allergens sequences from the raw fruit to the fully folded biotinylated protein product.
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