8014-42-4Relevant articles and documents
Mechanochemical synthesis of CuO/MgAl2O4 and MgFe2O4 spinels for vanillin production from isoeugenol and vanillyl alcohol
Rahmanivahid, Behgam,de Dios, Maria Pinilla,Haghighi, Mohammad,Luque, Rafael
, (2019)
CuO/MgAl2O4 and CuO/MgFe2O4 catalysts were successfully synthesized with the use of spinel supports by a very simple and low-cost mechanochemical method. High-speed ball-milling was used to synthesize these catalyst supports for the first time. Materials were subsequently characterized by using XRD, FESEM, TEM, EDS-Dot mapping, XPS, BET-BJH, and Magnetic Susceptibility to investigate the physical-chemical characteristics of the catalysts. Acidity evaluation results indicated that the catalyst with the Mg-Al spinel support had more acid sites. XRD results showed a successful synthesis of the catalysts with large crystal sizes. Both catalysts were used in isoeugenol oxidation and vanillyl alcohol to vanillin reactions, with the CuO/MgAl2O4 showing optimum results. This catalyst provided 67% conversion (74% selectivity) after 2 h and this value improved to 81% (selectivity 100%) with the second reaction after 8 h. The CuO/MgFe2O4 catalyst in the first reaction after five hours revealed 53% conversion (47% selectivity) and after eight hours with the second reaction, the conversion value improved to 64% (100% selectivity). In terms of reusability, CuO/MgAl2O4 showed better results than the CuO/MgFe2O4 catalyst, for both reactions.
Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis
Alvigini, Laura,Fraaije, Marco W.,Gran-Scheuch, Alejandro,Guo, Yiming,Mattevi, Andrea,Saifuddin, Mohammad,Trajkovic, Milos
, p. 3225 - 3233 (2021/10/04)
The vanillyl-alcohol oxidase (VAO) family is a rich source of biocatalysts for the oxidative bioconversion of phenolic compounds. Through genome mining and sequence comparisons, we found that several family members lack a generally conserved catalytic aspartate. This finding led us to study a VAO-homolog featuring a glutamate residue in place of the common aspartate. This 4-ethylphenol oxidase from Gulosibacter chungangensis (Gc4EO) shares 42 % sequence identity with VAO from Penicillium simplicissimum, contains the same 8α-N3-histidyl-bound FAD and uses oxygen as electron acceptor. However, Gc4EO features a distinct substrate scope and product specificity as it is primarily effective in the dehydrogenation of para-substituted phenols with little generation of hydroxylated products. The three-dimensional structure shows that the characteristic glutamate side chain creates a closely packed environment that may limit water accessibility and thereby protect from hydroxylation. With its high thermal stability, well defined structural properties and high expression yields, Gc4EO may become a catalyst of choice for the specific dehydrogenation of phenolic compounds bearing small substituents.
PhIO-Mediated oxidative dethioacetalization/dethioketalization under water-free conditions
Du, Yunfei,Ouyang, Yaxin,Wang, Xi,Wang, Xiaofan,Yu, Zhenyang,Zhao, Bingyue,Zhao, Kang
, p. 48 - 65 (2021/06/16)
Treatment of thioacetals and thioketals with iodosobenzene in anhydrous DCM conveniently afforded the corresponding carbonyl compounds in high yields under water-free conditions. The mechanistic studies indicate that this dethioacetalization/dethioketalization process does not need water and the oxygen of the carbonyl products comes from the hypervalent iodine reagent.
