Purification and characterization of halohydrin hydrogen-halide lyase from a recombinant Escherichia coli containing the gene from a Corynebacterium sp.


An enzyme catalyzing the interconversion of 1,3-dichloro-2-propanol (DCP) to epichlorohydrin (ECH) was purified from Escherichia coli JM109/ pST001, which carried the gene from Corynebacterium sp. 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… (More)
DOI: 10.1007/BF00170187


5 Figures and Tables