Native polyacrylamide gels of extracellular proteins produced by several Streptomyces isolates grown with suberin were assayed in situ for esterase activity. Two pathogenic isolates of Streptomyces scabies from different geographical regions were found to produce a similar esterase activity that was not produced by nonpathogenic strains. After treatment with EDTA, suberin no longer induced esterase production. Expression was restored when EDTA-treated suberin was supplemented with zinc. The optimal concentration of zinc required for esterase production was 2 μM. This esterase was purified from one of the pathogenic isolates and characterized. The enzyme was 38,000 daltons when determined by gel filtration on Sephadex G-100 and 36,000 daltons when determined by denaturing polyacrylamide gel electrophoresis. The esterase showed maximal activity in sodium phosphate buffer above pH 8.0, was stable to temperatures of up to 60° C, and had an apparent K(m) of 125 μM p-nitrophenyl butyrate.