This paper presents mathematical and computational modelling of kinetics of a bioelectroanalytical system based on the interfacial action of hydrolytic enzyme. A system of non-linear differential equations with diffusion is used to describe the kinetics of Termomyces lanuginosa lipase (TLL) catalyzed hydrolysis of L-ascorbic acid palmitate (AAP). The system was solved numerically, and the kinetic prameters of AAP hydrolysis by the enzyme were determined. The experimental and modelling results show linear dependence of the rate of AAP hydrolysis on the TLL concentration. Complex dependence of the initial rate of bioelectrocatalytic current increase on the thickness of total diffusion layer (hydrodynamic diffusion layer plus thickness of dialysis membrane on the electrode surface) is also demonstrated and explained. [...]
This paper addresses the effects of the concentration of lipases, temperature and solvent on the enzymatic acetylation of primary amines. (±)-Heptan-2-amine 1, (±)-4-phenylbutan-2-amine 2, (±)-1,2,3,4-tetrahydronaphthalen-1-amine 3 and (±)-2-methylcyclohexan-1-amine 4 were acetylated using 11 lipases to obtain amides under orbital shaking and microwave radiation. Under microwave radiation the same amines were acetylated only using the CALB. (±)-Heptan-2-amine 1 was subjected to kinetic resolution, under orbital shaking for 7 h employing CALB and ethyl acetate as acylating agent, and converted into (R)-N- (heptan-2-yl)acetamide 5 (c = 42%, 88% eep, hexane c = 52%, 81% eep, isopropyl ether; c = 40%, 65% eep, toluene). The reaction was fast (15 s) under microwave radiation in hexane and yielded acetamide 4 in high conversion (c = 91%), but without selectivity (5% eep).
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