Cereal Chem 46:656 - 662.  |  VIEW ARTICLE
Purification and Properties of Soybean Allantoinase.

L. C. Wang and R. L. Anderson. Copyright 1969 by the American Association of Cereal Chemists, Inc. 

Soybean allantoinase was purified by ammonium sulfate precipitation, diethylaminoethyl cellulose chromatography, and gel filtration. The enzyme, which is present in soybean whey, was purified 671-fold from a pH 4.5 acetate buffer extract. The yield was more than 30%. Allantoinase has a sedimentation coefficient of 4.9S, which corresponds to a molecular weight of about 50,000. The enzyme has an optimum pH of 8.4, Km of 4.4 x 10(-2)M, and an optimum temperature at 70 C. Short heating of the buffer extract activates the enzyme; it is six times more active at 70 C. than at 25 C. but it inactivates twice as fast at temperatures higher than 70 C., its optimum activation point.