T. Uchikoba et al., Isolation and some properties of a serine protease from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam., BIOS BIOT B, 64(3), 2000, pp. 623-624
An endopeptidase (Cudrania protease) with molecular mass of 76 kDa has been
purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam
. The enzyme was stable between pH 6 and 10 at 30 degrees C for 60 min. The
enzyme activity was inhibited by diisopropyl fluorophosphate, chymostatin,
and aprotinin, but not by EDTA or pepstatin. These results indicated that
the enzyme was a serine protease.