Document Detail


Vanadium containing bromoperoxidase: An example of an oxidoreductase with high operational stability in aqueous and organic media.
MedLine Citation:
PMID:  18581447     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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.
Authors:
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:
Type:  Journal Article    
Journal Detail:
Title:  Biotechnology and bioengineering     Volume:  30     ISSN:  0006-3592     ISO Abbreviation:  Biotechnol. Bioeng.     Publication Date:  1987 Oct 
Date Detail:
Created Date:  2008-06-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7502021     Medline TA:  Biotechnol Bioeng     Country:  United States    
Other Details:
Languages:  eng     Pagination:  607-10     Citation Subset:  -    
Affiliation:
Laboratory of Biochemistry, University of Amsterdam, P.O. Box 20151, 1000 HD Amsterdam and Biotechnological Centre, University of Amsterdam, Amsterdam.
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