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Open Access Green as soon as Postprint is submitted to ZB.
A mechanistic study into the epoxidation of carboxylic acid and alkene in a mono, di-acylglycerol lipase.
Biochem. Biophys. Res. Commun. 460, 392-396 (2015)
More and more industrial chemistry reactions relies on green technologies. Enzymes are finding increasing use in diverse chemical processes. Epoxidized vegetable oils have recently found applications as plasticizers and additives for PVC production. We report here an unusual activity of the M. globosa lipase (SMG1) that is able to catalyze epoxidation of alkenes. SMG1 catalyzes formation of peroxides from long chain carboxylic acids that subsequently react with double bonds of alkenes to produce epoxides. The SMG1 is selective towards carboxylic acids and active also as a mutant lacking hydrolase activity. Moreover we present previously unobserved mechanism of catalysis that does not rely on acyl-substrate complex nor tetrahedral intermediate. Since SMG1 lipase is activated by allosteric change upon binding to the lipophilic-hydrophilic phase interface we reason that it can be used to drive the epoxidation in the lipohilic phase exclusively.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
M. Globosa Lipase ; Alkene ; Carboxylic Acid ; Epoxidation ; Mechanism ; Oil; Epoxidized Sunflower Oil; Malassezia-globosa; Soybean Oil; Diacylglycerol Lipase; Hydrogen-peroxide; Perhydrolysis; Catalysis; Alpha
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 460,
Issue: 2,
Pages: 392-396
Publisher
Elsevier
Publishing Place
San Diego
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)