Lipase and esterase-catalyzed acylation of hetero-substituted nitrogen nucleophiles in water and organic solvents.
The lipase- and esterase-catalyzed acylations of hydroxylamine and hydrazine derivatives with octanoic acid and ethyl octanoate are described. The influence of solvent and nucleophile on the initial reaction rate was investigated for a number of free and immobilized enzymes. Initial rates were highest in water, but the overall productivity was optimal in dioxane. Octanoic acid (250 g/L) was converted for 93% into the hydroxamic acid in 36 h with only 1% (w/w) Candida antarctica lipase B (Novozym 435) in dioxane at 40 degrees C. This translates to a catalyst productivity of 68.5 g. g(-1). day(-1) and a space time yield of 149 g. L(-1). day(-1), unprecedented figures in the direct reaction of an acid with a nitrogen nucleophile in an organic solvent.
Hacking
M A
MA
Laboratory of Organic Chemistry, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
Akkus
H
H
van Rantwijk
F
F
Sheldon
R A
RA
D000215:Acylation; D001709:Biotechnology / Q000379:methods*; D002175:Candida / Q000378:metabolism; D002273:Carcinogens / Q000378:metabolism; D004950:Esterases / Q000378:metabolism*; D006834:Hydrazines / Q000378:metabolism; D019811:Hydroxylamine / Q000378:metabolism; D008049:Lipase / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D012997:Solvents; D014867:Water
D002273:Carcinogens; D006834:Hydrazines; D012997:Solvents; D014867:Water; C029424:hydrazine; D019811:Hydroxylamine; D004950:Esterases; D008049:Lipase; D009584:Nitrogen