PARTIAL PURIFICATION AND CHARACTERIZATION OF PEPTIDE HYDROLASES FROM GERMINATED WHEAT

Peptide hydrolases from germinated wheat were purified by methods developed previously for barley peptide hydrolases. Comparisons of the wheat enzymes for their thermal stability, pH optima, stability at various pH values, kinetic constants, and effects of metal ions revealed that wheat possesses a neutral peptide hydrolase with properties very similar to those of barley hydrolase B. After considerable purification the acidic peptide hydrolase fraction of wheat appeared to contain two peptide hydrolases, one that was similar to barley peptide hydrolase A and a second which was more resistant to low pH and thermal denaturation. © 1968.