[en] A commercial crude sulfatase from snail (Helix pomatia) was purified by ion exchange affinity, HPLC, gel-filtration chromatography. The enzyme isolated. which was ca. 37-folcl more active than the commercial one was covalently immobilizcd on nyon 6.6 by the cross linking method. Immobilized sulfatase was usecl to produce some desulfo-glucosinolates (DSGLs) on the gram-scale. starting fiom glucotropaeolin. glucoraphenin ancl épiprogoitrin ancl for HPLC analyses of glucosinolates (GLs) containecl in cruciferous material and rapeseecl in particular. The
immobilized enzyme as well as allowing the standarclization of the HPLC methocl for GLs analysis seems to be an efflcient system for producing DSGLs which are interesting starting materials to prepare bio-active structures through further chemical modilications.
