pBIC2短芽孢桿菌表達(dá)載體質(zhì)粒

TheBrevibacillus Expression System is an efficient system for producing secreted proteins and
is ideal for eukaryotic recombinant protein expression.Brevibacillus choshinensis is a grampositive bacterium well-suited for heterologous protein expression and is capable of producing
high yields of active protein. This system offers the following advantages:
?Extracellular secretion of large volumes of protein
?Simple procedures for genetic manipulation and culturing
?Almost no detectable protease activity
?Production of active protein
?Safe host bacteria
Examples of protein production using this system are shown in Table 1. High expression of
biologically active protein (enzymes, antigens, and cytokines) was obtained regardless of gene
origin (bacterial, archaea, or eukaryotic). In particular, eukaryotic secretory proteins often contain
disulfide (S-S) bonds and are generally difficult to produce in prokaryotic expression systems. The
B. choshinensis Host-Vector System can produce high yields of secretory proteins, including those
with disulfide bonds.

The high transformation efficiency ofBrevibacillus makes cloning target genes simple. The
BIC (Brevibacillus in vivo Cloning) method used in this system allows expression plasmids to
be constructed by simply by mixing PCR fragments with the vector DNA and transforming the
mixture into the host bacteria.
In addition, culturing methods for protein production are also simple. Culturing for production
of the target protein uses one of two types of media (see V-8. Composition of Medium). For
secretory protein expression, medium is inoculated with transformed host bacteria, and the
target protein accumulates in the culture supernatant. After culturing, the protein-containing
solution can be obtained by removing the cells by centrifugation, and protein can be further
purified as needed.

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