Secretion of Escherichia coli Aminopeptidase P in Bacillus subtilis Using the Prepro-Structure Coding Region of Subtilisin Amylosacchariticus

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Secretion vector which contained the promoter, prepro- and mature protein coding regions of subtilisin Amylosacchariticus gene (aprA) was constructed, and the Escherichia coli aminopeptidase P structure gene (pepP) was inserted into the secretion vector. When the resultant chimeric plasmids were transferred into Bacillus subtilis ISW1214,and the transformants were aerobically cultivated, the aminopeptidase P gene was expressed and the enzyme was secreted into the culture medium. The secreted enzyme was indistinguishable immunologically from that of E. coli by a double immunodiffusion test. The molecular weight of the secreted enzyme was about 200,000 and 50,000 by gel filtration and SDS-PAGE, respectively. These results suggested that the enzyme was excreted as a tetramer form. The substrate specificity of the secreted aminopeptidase P from B. subtilis was also quite similar to that of enzyme from E. coli.
社団法人日本生物工学会の論文
1989-10-25