ethyl-ferulate has been researched along with methyl-ferulate* in 3 studies
3 other study(ies) available for ethyl-ferulate and methyl-ferulate
| Article | Year |
|---|---|
The Structure-Antioxidant Activity Relationship of Ferulates.
The antioxidant activity of ferulic acid ( Topics: Acrolein; Antioxidants; Caffeic Acids; Coumaric Acids; Molecular Structure; Oxidation-Reduction; Structure-Activity Relationship | 2017 |
Formation of ethyl ferulate from feruloylated oligosaccharide by transesterification of rice koji enzyme under sake mash conditions.
Formation of ethyl ferulate (EF) and ferulic acid (FA) under sake mash conditions was studied using feruloylated oligosaccharide (FO), prepared from rice grains, as the substrate for rice koji enzyme. EF and FA were produced from FO over six times faster than from alkyl ferulates however, under the same ethanol concentration, only small differences were observed between the EF/FA ratios when either FO or methyl ferulate were used as substrates. Esterification and hydrolysis of FO or methyl ferulate showed similar pH dependencies and similar EF/FA ratios for each substrate in all of the pH ranges tested. Ethanol concentration clearly affected the EF/FA ratio; the ratio increased as ethanol concentration increased. Formation of EF and FA in the sake mash simulated rice digest was accelerated by addition of exogenous FO. These results indicated that supply of FO to sake mash is a crucial step for EF and FA formation, and ethanol is an influencing factor in the EF/FA ratio. The rice koji enzyme reaction suggested that EF and FA are formed through a common feruloylated enzyme intermediate complex by transesterification or hydrolysis, and these reactions occur competitively. Topics: Alcoholic Beverages; Caffeic Acids; Coumaric Acids; Esterification; Ethanol; Hydrogen-Ion Concentration; Hydrolysis; Oligosaccharides; Oryza | 2016 |
Discovery of novel feruloyl esterase activity of BioH in Escherichia coli BL21(DE3).
To characterize a novel feruloyl esterase from Escherichia coli BL21 DE3.. The gene encoding BioH was cloned and overexpressed in E. coli. The protein was purified and its catalytic activity was assessed. BioH exhibited feruloyl esterase activity toward a broad range of substrates, and the corresponding kinetic constants for the methyl ferulate, ethyl ferulate, and methyl p-coumarate substrates were: K m values of 0.48, 6.3, and 1.9 mM, respectively, and k cat /K m values of 9.3, 3.8, and 3.8 mM(-1) s(-1), respectively.. Feruloyl esterase from E. coli was expressed for the first time. BioH was confirmed to be a feruloyl esterase. Topics: Caffeic Acids; Carboxylic Ester Hydrolases; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Kinetics; Substrate Specificity | 2016 |