Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent
Biotechnology Letters, ISSN: 0141-5492, Vol: 26, Issue: 23, Page: 1815-1819
2004
- 62Citations
- 30Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations62
- Citation Indexes62
- 62
- CrossRef56
- Captures30
- Readers30
- 30
Article Description
Chloroperoxidase from Caldariomyces fumago catalyses the oxidation of 1,2-dihydronaphthalene to (1R,2R)-(+)-dihydroxytetrahydronaphthalene in homogenous citrate buffer/ionic liquid mixtures, using t-butyl hydroperoxide as O donor. It tolerates up to 30% (v/v) 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate. The enzyme activity in these ionic liquid co-solvent systems is retained for 24 h, but it falls to 3 h using non-ionic organic solvents such as t-BuOH or acetone.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=13244270107&origin=inward; http://dx.doi.org/10.1007/s10529-004-5087-6; http://www.ncbi.nlm.nih.gov/pubmed/15672220; http://link.springer.com/10.1007/s10529-004-5087-6; http://www.springerlink.com/index/10.1007/s10529-004-5087-6; http://www.springerlink.com/index/pdf/10.1007/s10529-004-5087-6; https://dx.doi.org/10.1007/s10529-004-5087-6; https://link.springer.com/article/10.1007/s10529-004-5087-6
Springer Science and Business Media LLC
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