Lipase and esterase-catalyzed acylation of hetero-substituted nitrogen nucleophiles in water and organic solvents

✍ Scribed by Michiel A. P. J. Hacking; Hüseyin Akkus; Fred van Rantwijk; Roger A. Sheldon

• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 110 KB
• Volume: 68
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(20000405)68:1<84::aid-bit10>3.0.co;2-5

✦ Synopsis

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.