The demand for proteins with special purposes increases
significantly, for example, special proteins are in good need in development of
sensitive, specific and reliable differential diagnostic assays. To meet such
huge demand, proteins of interest can be expressed in either prokaryotic or
eukaryotic cells, like Escherichia coli, to produce recombinant proteins.
However, this is not an easy task and is often costly. Purification ofrecombinant proteins from plant biomass currently accounts for almost 80% ofproduction cost. A series of difficulties may be encountered in purification.
For instance, purified proteins from a host may accumulate in low titers and
may be mixed with infection or form protein aggregates. Therefore a
purification scheme usually includes many steps, such as affinity
chromatography, precipitation, protecting of recombinant proteins from
degradation with stabilizer, centrifugation and so on.
In order to develop an efficient and cost-effective
purification scheme, many efforts have been made and much has been achieved infinding the factors that affect protein purification. At codon optimization
level, N-terminal rare codons increase expression with some reservation.
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