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Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation
dc.creator | Milivojević, Ana | |
dc.creator | Ćorović, Marija | |
dc.creator | Simović, Milica | |
dc.creator | Banjanac, Katarina | |
dc.creator | Vujisić, Ljubodrag V. | |
dc.creator | Veličković, Dušan | |
dc.creator | Bezbradica, Dejan | |
dc.date.accessioned | 2021-03-10T13:24:26Z | |
dc.date.available | 2021-03-10T13:24:26Z | |
dc.date.issued | 2017 | |
dc.identifier.issn | 1369-703X | |
dc.identifier.uri | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3593 | |
dc.description.abstract | Solubility and stability of flavonoid glycosides, valuable natural constituents of cosmetics and pharmaceuticals, could be improved by lipase-catalyzed acylation. Focus of this study was on development of eco-friendly process for the production of flavonoid acetates. By using phloridzin as model compound and triacetin as acetyl donor and solvent, 100% conversion and high productivity (23.32 gl(-1) day(-1)) were accomplished. Complete conversions of two other glycosylated flavonoids, naringin and esculin, in solvent-free system were achieved, as well. Comprehensive kinetic mechanism based on two con-secutive mono-substrate reactions was established where first one represents formation of flavonoid monoacetate and within second reaction diacetate is being produced from monoacetate. Both steps were regarded as reversible Michaelis-Menten reactions without inhibition. Apparent kinetic parameters for two consecutive reactions (V-m constants for substrates and products and Km constants for forward and reverse reactions) were estimated for three examined acetyl acceptors and excellent fitting of experimental data (R-2 gt 0.97) was achieved. Obtained results showed that derived kinetic model could be applicable for solvent-free esterifications of different flavonoid glycosides. It was valid for entire transesterification course (72 h of reaction) which, combined with complete conversions and green character of synthesis, represents firm basis for further process development. | en |
dc.publisher | Elsevier Science Bv, Amsterdam | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS// | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172053/RS// | |
dc.rights | restrictedAccess | |
dc.source | Biochemical Engineering Journal | |
dc.subject | Flavonoid acetylation | en |
dc.subject | Lipase | en |
dc.subject | Solvent-free | en |
dc.subject | Kinetic parameters | en |
dc.subject | COPASI | en |
dc.title | Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 115 | |
dc.citation.other | 128: 106-115 | |
dc.citation.rank | M21 | |
dc.citation.spage | 106 | |
dc.citation.volume | 128 | |
dc.identifier.doi | 10.1016/j.bej.2017.09.018 | |
dc.identifier.scopus | 2-s2.0-85030172007 | |
dc.identifier.wos | 000417008900012 | |
dc.type.version | publishedVersion |