61016-96-4Relevant academic research and scientific papers
Hydroxy functional acrylate and methacrylate monomers prepared via lipase-catalyzed transacylation reactions
Popescu, Dragos,Hoogenboom, Richard,Keul, Helmut,Moeller, Martin
, p. 80 - 89 (2010)
Candida antarctica lipase B (CAL-B, Novozyme 435) catalyzes the transacylation of methyl acrylate and methyl methacrylate with diols and triols in 2-methyl-2-butanol at 50 °C. Under the experimental conditions, up to 70 mol% of the acyl donor methyl acrylate was converted. Methyl methacrylate is the less efficient acyl donor (up to 60 mol%) due to the higher sterical hindrance in the enzymatic transacylation. Under the reaction conditions high yields of the mono-acylated products are obtained, which contain minor amounts of bis(meth)acrylates. In addition it was observed that Novozyme 435 catalyzes regioselectively the acylation of the primary hydroxyl groups. In comparison with the chemical catalyzed route no selectivity was observed for unsubstituted diols. For substituted diols more mono-acylated product was formed in the lipase-catalyzed reaction than in the chemical catalyzed reaction.
Runge-Kutta analysis for optimizing the Zn-catalyzed transesterification conditions of MA and MMA with diols to maximize monoesterified products
Kato, Taito,Akebi, Shin-Ya,Nagae, Haruki,Yonehara, Koji,Oku, Tomoharu,Mashima, Kazushi
, p. 6975 - 6986 (2021/11/17)
Terminal hydroxylated acrylates and methacrylates were prepared by catalytic transesterification of acrylates and methacrylates with diols catalyzed by a system of a tetranuclear zinc alkoxide, [Zn(tmhd)(OMe)(MeOH)]4 (1a), with 4 equiv. of 2,2′-bipyridine (L1). The reaction time to reach the equilibrium state was analyzed by kinetic studies and a curve-fitting analysis based on the Runge-Kutta method for optimizing the best reaction conditions for mono-esterification. In addition to these kinetic analyses, DFT calculations estimated a proposed mechanism of the catalytic transesterification. This journal is
