Vanadate(V)-dependent bromoperoxidase I (Ascophyllum nodosum) was immobilized on magnetic micrometre-sized particles in quantitative yields, with up to 40% retention of initial bromoperoxidase (BPO) activity. The immobilized enzyme was stable with a half-life time of about 160 days. It served as reusable catalyst for bromide oxidation with H2O2 in up to 14 consecutive experiments. Reactivity that resulted from enzymatic bromide oxidation was applicable for methyl pyrrole-2-carboxylate conversion into derivatives of naturally occurring compounds (e.g. from Agelas oroides) with product selectivity of up to 75%.
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Wischang et al. (2010) studied this question.
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