ABSTRACT
The production of stable and soluble proteins is one of the most important steps before structural and functional studies of biological importance. An alternative to obtaining native enzymes is the purification of recombinant enzymes after expression of genes of interest in a heterologous host, in particular the bacteria Escherichia coli. One of the advantages of this approach is to quickly produce bacterial biomass likely to contain the proteins of interest. This protocol describes the different steps to cloning, expression, and purification of protein identified in the brown alga Ectocarpus siliculosus.
Keywords: Brown algae, heterologous overexpression, recombinant protein, cloning, purification
