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J. Biochem, 1996, Vol. 119, No. 4 711-718
© 1996 Japanese Biochemical Society

research-article

Partial Purification and Characterization of a Novel Soybean Protease Which is inhibited by Kunitz and Bowman-Birk Trypsin Inhibitors

Shimpei Morita1, Masami Fukase, Kumiko Hoshino, Yoichi Fukuda, Masami Yamaguchi and Yuhei Morita

Central Research Institute, Fuji Oil Co 4-3 Kinunodai, Yawara-mura, Tsukuba-gun, Ibaruki 300-24

1To whom correspondence should be addressed. Tel: +81-297-52-6321, Fax: +81-297-52-6326, e-mail: moritaj{at}fujioil.co.jp

A novel serine protease has been partially purified from dry seeds of the soybean (Glycine max;) cultivar Keburi by cryoprecipitation at pH 6.4, fractional precipitation with ammonium sulfate, and a series of column chromatographic procedures on DEAE-Sepharose, SP-Sepharose, and Arginine-Sepharose 4B. Some properties of the purified enzyme were studied. The protease hydrolyzed the native storage globulins of soybean seeds, such as the {alpha} subunit of ß-conglycinin, at a pair of arginine residues, Argl26-Argl27. The proteolysis of the {alpha} subunit in the purified {alpha}2ß molecule of ß-conglycinin apparently followed first order kinetics. The enzyme was inhibited by both soybean Kunitz trypsin inhibitor and Bowman-Birk proteinase inhibitor in a competitive manner. Moreover, the enzyme could catalyze the specific proteolysis of the A3 polypeptide of the purified G5 glycinin at the Arg99-Glyl00 linkage, or the carboxyl side of the Arg98-Arg99 paired basic residues.


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