{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu Y"],"funding":["Modern Agro-industry Technology Research System of China","Shen Lan Young scholars program of Jiangsu University of Science and Technology","Natural Science Foundation of China","Six Talent Peaks Project of Jiangsu Province","Qing Lan Project of Jiangsu Province"],"pagination":["E72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6155643"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(1)"],"pubmed_abstract":["It is widely believed that lipases in ionic liquids (ILs) possess higher enzyme activity, stability and selectivity; however, reaction equilibrium is always limited by product inhibition, and the product is difficult to separate from non-volatile ILs using distillation. To solve this problem, using trialkylphosphine oxide (TOPO) as a complexing agent, a novel biphase of reactive solvent and IL was firstly reported for caffeic acid phenethyl ester (CAPE) production from methyl caffeate (MC) and 2-phenylethanol (PE) catalyzed by lipase <i>via</i> transesterification. The effects of the reaction parameters and their action mechanism were investigated, and the inhibition of CAPE against bacterial wilt pathogen <i>Ralstonia solanacearum</i> was firstly measured. The MC conversion of 98.83% ± 0."],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Cooperative Reinforcement of Ionic Liquid and Reactive Solvent on Enzymatic Synthesis of Caffeic Acid Phenethyl Ester as an In Vitro Inhibitor of Plant Pathogenic Bacteria."],"pmcid":["PMC6155643"],"funding_grant_id":["Year of 2015","2015-NY-018","CARS-22","Year of 2014","21206061"],"pubmed_authors":["Liu X","Wu FA","Wang C","Xiao W","Sheng S","Wang J","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"Cooperative Reinforcement of Ionic Liquid and Reactive Solvent on Enzymatic Synthesis of Caffeic Acid Phenethyl Ester as an In Vitro Inhibitor of Plant Pathogenic Bacteria.","description":"It is widely believed that lipases in ionic liquids (ILs) possess higher enzyme activity, stability and selectivity; however, reaction equilibrium is always limited by product inhibition, and the product is difficult to separate from non-volatile ILs using distillation. To solve this problem, using trialkylphosphine oxide (TOPO) as a complexing agent, a novel biphase of reactive solvent and IL was firstly reported for caffeic acid phenethyl ester (CAPE) production from methyl caffeate (MC) and 2-phenylethanol (PE) catalyzed by lipase <i>via</i> transesterification. The effects of the reaction parameters and their action mechanism were investigated, and the inhibition of CAPE against bacterial wilt pathogen <i>Ralstonia solanacearum</i> was firstly measured. The MC conversion of 98.83% ± 0.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Jan","modification":"2026-06-07T06:37:18.286Z","creation":"2025-05-29T22:02:15.476Z"},"accession":"S-EPMC6155643","cross_references":{"pubmed":["28045451"],"doi":["10.3390/molecules22010072"]}}