| Vanadium containing bromoperoxidase: An example of an oxidoreductase with high operational stability in aqueous and organic media. | |
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MedLine Citation:
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PMID: 18581447 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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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. |
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Authors:
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E de Boer; H Plat; M G Tromp; R Wever; M C Franssen; H C van der Plas; E M Meijer; H E Schoemaker |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biotechnology and bioengineering Volume: 30 ISSN: 0006-3592 ISO Abbreviation: Biotechnol. Bioeng. Publication Date: 1987 Oct |
Date Detail:
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Created Date: 2008-06-26 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7502021 Medline TA: Biotechnol Bioeng Country: United States |
Other Details:
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Languages: eng Pagination: 607-10 Citation Subset: - |
Affiliation:
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Laboratory of Biochemistry, University of Amsterdam, P.O. Box 20151, 1000 HD Amsterdam and Biotechnological Centre, University of Amsterdam, Amsterdam. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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