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Vanadium containing bromoperoxidase: An example of an oxidoreductase with high operational stability in aqueous and organic media
Author(s) -
de Boer E.,
Plat H.,
Tromp M. G. M.,
Wever R.,
Franssen M. C. R.,
van der Plas H. C.,
Meijer E. M.,
Schoemaker H. E.
Publication year - 1987
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260300504
Subject(s) - vanadium , chemistry , aqueous solution , oxidoreductase , aqueous medium , inorganic chemistry , chromatography , organic chemistry , enzyme
The conversion is described of phenolsulphonephtalein (phenol red) to 3,3′,5,5′‐tetrabromophenolsulphonephthalein (bromophenol blue) by bromoper‐oxidase from the brown alga Ascophyllum nodosum. This reaction provides a convenient assay for the detection of bromoperoxidase activity in vitro. Bromoperoxidase was shown to be stable under turnover conditions for three weeks at room temperature, catalyzing the bromination of phenol red into bromophenol blue. When stored at room temperature in organic sol vents such as acetone, methanol, ethanol [present up to 60% (v/v)], and 1‐propanol [40% (v/v)], bromoperoxidase was stable for more than one month. As far as we know this is the first example of an oxidoreductase which displays such great stability. This enhances the applicability of the enzyme in organic synthesis.