PARTIAL PURIFICATION AND CHARACTERIZATION OF AN AMIDOHYDROLASE FROM SOYBEAN

A soluble enzyme with amidohydrolase activity was isolated from the roots of soybean seedlings and purified 45-fold by ammonium sulfate fractionation, gel filtration and cellulose ion-exchange chromatography. The enzyme hydrolyzed primarily Nα-benzoyl-dl-arginine p-nitroanilide and to a slight extent the p-nitroanilides of glycine and l-leucine, but it did not hydrolyze casein, Azocoll and the p-nitroanilides of l-lysine, l-cystine, succinyl-l-phenylalanine and glutaryl-l-phenylalanine. The apparnet Km for Nα-benzoyl-dl-arginine p-nitroanilide was 5·78 × 10-5 M. The effects of temperature, pH, metal ions and sulfhydryl reagents on the enzyme were also investigated. © 1970.