Characterization of Novel Cysteine Proteases from Germinating Cotyledons of Soybean (Glycine max (L.) Merrill).

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The enzymatic properties of novel cysteine proteases D 3-α and β which were purified from germinating soybean cotyledons were investigated. The enzyme activities were exhibited in the presence of a thiol reagent, such as 2-mercaptoethanol, and apparently inhibited by E-64, a cysteine protease inhibitor. Hydrolytic activities toward carbobenzoxy-Phe-Arg-MCA were detected at a pH above 4.0. The optimum temperature for activities was about 40°C. The isoelectric point of D 3-α and β was 4.4 and 4.7, respectively. The molecular mass of D 3-α and β, measured by MALDI/TOF mass spectrometry, was 26, 178 and 26, 429 Da, respectively. The substrate specificities of the enzymes were examined using peptide-MCAs and peptides, and cathepsin L-like broad specificity was observed at pH 4.0. These results demonstrated that these enzymes are cysteine endopeptidases [EC 3. 4. 22.-] like papain [EC 3. 4. 22. 2].
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