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Design and production of genetically modified soybean protein with anti‐hypertensive activity by incorporating potent analogue of ovokinin(2–7)
Author(s) -
Matoba Nobuyuki,
Doyama Naomi,
Yamada Yuko,
Maruyama Nobuyuki,
Utsumi Shigeru,
Yoshikawa Masaaki
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02434-6
Subject(s) - protein subunit , trypsin , peptide , recombinant dna , biochemistry , chymotrypsin , mutagenesis , in vivo , chemistry , escherichia coli , ion chromatography , in vitro , enzyme , biology , microbiology and biotechnology , gene , mutation
The potent anti‐hypertensive peptide, RPLKPW, has been designed based on the structure of ovokinin(2–7). The sequence encoding this peptide was introduced into three homologous sites in the gene for soybean β‐conglycinin α′ subunit. The native α′ subunit as well as the modified, RPLKPW‐containing α′ subunit were expressed in Escherichia coli , recovered from the soluble fraction and then purified by ion‐exchange chromatography. The RPLKPW peptide was released from recombinant RPLKPW‐containing α′ subunit after in vitro digestion by trypsin and chymotrypsin. Moreover, the undigested RPLKPW‐containing α′ subunit given orally at a dose of 10 mg/kg exerted an anti‐hypertensive effect in spontaneously hypertensive rats, unlike the native α′ subunit. These results provide evidence for the first time that a physiologically active peptide introduced into a food protein by site‐directed mutagenesis could practically function in vivo even at a low dose.