Lipase catalyzed synthesis of peroxycarboxylic acids and lipase mediated oxidations.

doi:10.1016/S0040-4020(01)81232-1

Tetrahedron

Volume 48, Issue 22, 1992, Pages 4587-4592

https://doi.org/10.1016/S0040-4020(01)81232-1 Get rights and content

Abstract

Lipase catalyzed synthesis of long chain peroxycarboxylic acids from hydrogen peroxide and free carboxylic acid was investigated. A 51% yield of peroxytetradecanoic acid was achieved when using a two phase system of toluene and water. The peroxy acids thus formed were applied for in situ oxidation of alkenes, in general leading to high yields of the corresponding epoxide. For example, a quantitative yield of cyclohexene oxide and a 94% yield of 1-hexadecene oxide was achieved in a solvent-free process.

Lipase catalyzed synthesis of long chain peroxycarboxylic acids from hydrogen peroxide and free carboxylic acid was investigated. A 51% yield of peroxytetradecanoic acid was achieved when using a two phase system of toluene and water. The peroxy acids thus formed were applied for in situ oxidation of alkenes, for example, a quantitative yield of cyclohexene oxide and a 94% yield of 1-hexadecene oxide was achieved in a solvent-free process.

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Soapstock recovery and manipulation represent one of the most burdensome aspects of the vegetable seed oil refining industry. In particular, soapstock splitting requires high amounts of concentrated acid and produces a low-value mixture of triglycerides and free fatty acids (oleins or acid oil), as well as huge volumes of acidulated wastewater. Oleins are currently converted into biodiesel or supplied to biodigesters, but alternative procedures to afford high-value products are sought after by the vegetable seed oil industry. In this paper, the valorization of soapstock from high-oleic sunflower oil refinement is investigated by biocatalytic methods. First, lipases are used to catalyze an efficient soapstock splitting, and reduce the environmental load of the procedure. Then, the high content of oleic acid (60–80%) is exploited by promoting its oxidative cleavage. Self-epoxidation of oleic acid by lipase-mediated perhydrolysis in the presence of H₂O₂ affords the corresponding epoxide, which is subsequently hydrolyzed to the diol derivative and oxidized to commercially valuable azelaic and pelargonic acids. The cleavage is performed using only sodium hypochlorite as an inexpensive and efficient oxidant. Epoxidation and glycol cleavage are optimized by a statistical approach and implemented under continuous-flow conditions to increase yields and productivity.
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Recently the idea of constructing “supramolecular enzyme systems” realized in the so-called “coimmobilized multienzymatic systems” strategy. The most fascinating example is the combined assay of a mixture of native LPP, glycerol kinase (from Cellulomonas) and glycerol-3-phosphate oxidase (from Aerococcus viridans) linked by glutaraldehyde to chitosan (as shell for inorganic nanoparticle core). This material was placed on a Pt-electrode as biosensor and was successfully applied for amperometric determination of the triglyceride level in the serum of healthy and diseased person. Thus, the whole innovative research-production sequence is described by Aggarwal V. and Pundir C.S.: from simple components to advanced material and further biomedical application.
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¹: Present address: Department of Organic Chemistry, Royal Institute of Technology, S-100 44 Stockholm, Sweden.

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Lipase catalyzed synthesis of peroxycarboxylic acids and lipase mediated oxidations.

Abstract

Trends in Biotechnology

Tetrahedron lett.

J. Chem. Soc., Chem. Commun.

Mangia Synthesis