Abstract
Pseudomonas marginalis N6301 produced pectin lyase (EC 4.2.2.10) in the medium with cell lysis when the culture was treated with mitomycin C. We purified the enzyme by carboxymethylcellulose, hydroxylapatite, and gel-filtration column chromatographies. The enzyme had a molecular weight of 34,000 by SDS polyacrylamide gel electrophoresis and was mostly stable around pH 6.5. The optimum pH and temperature for the enzyme activity were 8.0 and 30°C, respectively. The activity was inhibited severely by 2 mM N-ethylmaleimide, maleic anhydride, and p-chloromercuriphenylsulfonic acid. Further, the pectin lyase produced in a medium containing glycerol was purified. The molecular weight of the enzyme was identical to that of the enzyme produced in the presence of mitomycin C.
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