SECRETED HYDROLASES FROM STREPTOMYCIN-RESISTANT STRAINS OF BACILLUS-INTERMEDIUS

Alkaline phosphatases and serine proteinases have been isolated from t he culture liquid of streptomycin-resistant strains of Bacillus interm edius using ion-exchange and affinity chromatography and FPLC. Substra te blotting and electrophoresis revealed two phosphatase forms with mo lecular masses of 40 and 50 kD. The enzyme had maximal activity at pH 9.5 and 50 degrees C and could cleave the phosphate moiety from a rang e of substrates. It is suggested that both forms of the phosphatase ar e products of processing that involves a serine proteinase. Two protei nases, with molecular masses of 29 and 33 kD, were purified to homogen eity from the culture liquid of B. intermedius S7. The protein from th e major peak was identical in its properties to an earlier described s erine proteinase. The minor peak was 5% of the major one. These enzyme s had different pH optima. Inhibitor analysis indicated that the minor peak is also a serine proteinase.