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>Purification and characterization of halohydrin hydrogen-halide lyase from a recombinantEscherichia colicontaining the gene from aCorynebacteriumsp.
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Purification and characterization of halohydrin hydrogen-halide lyase from a recombinantEscherichia colicontaining the gene from aCorynebacteriumsp.
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机译：Purification and characterization of halohydrin hydrogen-halide lyase from a recombinantEscherichia colicontaining the gene from aCorynebacteriumsp.
An enzyme catalyzing the interconversion of 1,3-dichloro-2-propanol (DCP) to epichlorohydrin (ECH) was purified fromEscherichia coliJM109/ pST001, which carried the gene fromCorynebacteriumsp. N-1074. The enzyme was crystallized by the addition of ammonium sulphate. The enzyme had a relative molecular mass (Mr) of about 105 000 and consisted of four subunits identical in Mr(approx. 28 000). The enzyme catalysed both the transformation of various halohydrins into the corresponding epoxides with liberation of halide and its reverse reaction. These facts indicated that the enzyme was halohydrin hydrogen-halidelyase.
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