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In this study, a multimer of the tandem angiotensin I\u2010converting enzyme inhibitory peptide (ACE\u2010IP) gene was directly transferred to a commercially available vector and the designed gene was expressed as a repeated peptide in <jats:italic>Escherichia coli<\/jats:italic> BL21(DE3)pLysS. The process further developed in our study was the construction of six\u2010repeated ACE\u2010IP synthetic genes and their direct insertion. Protein expression in inclusion bodies was confirmed by SDS\u2010PAGE and Western blot. Acid hydrolysis of inclusion bodies produced single\u2010unit peptides through cleavage of the aspartyl\u2010prolyl bonds. This cleaved recombinant peptide (rACE\u2010IP) was purified using immuno\u2010affinity chromatography followed by reversed phase\u2010HPLC. 105\u2013115 mg of the lyophilized recombinant peptide was obtained from 1 L <jats:italic>E. coli<\/jats:italic> culture. <jats:italic>In vitro<\/jats:italic> biological activity of rACE\u2010IP was indistinguishable from that of the natural peptide produced by hydrolysis in artificial gastric juice or by acidic hydrolysis. The rACE\u2010IP prepared by recombinant DNA technology and solid\u2010phase synthesis methods showed a similar IC<jats:sub>50<\/jats:sub>. This strategy could be used for the expression of important peptides, which have N\u2010terminal proline (P) and C\u2010terminal aspartic acid residues (D) for commercial applications, <jats:italic>e.g.<\/jats:italic> functional foods and drinks.<\/jats:p>","DOI":"10.1002\/biot.200800326","type":"journal-article","created":{"date-parts":[[2009,4,27]],"date-time":"2009-04-27T18:50:54Z","timestamp":1240858254000},"page":"1345-1356","source":"Crossref","is-referenced-by-count":16,"title":["Tandem multimer expression of angiotensin I\u2010converting enzyme inhibitory peptide in <i>Escherichia coli<\/i>"],"prefix":"10.1002","volume":"4","author":[{"given":"Hasan M.","family":"Fida","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoichi","family":"Kumada","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaaki","family":"Terashima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomohisa","family":"Katsuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shigeo","family":"Katoh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,9,23]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(70)90017-6"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.CIR.81.1.381"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.procbio.2005.06.032"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(88)81089-1"},{"key":"e_1_2_1_6_2","first-page":"163181","article-title":"Purification of secreted recombinant proteins from Escherichia coli.","volume":"12","author":"Le H. 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