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

Biotechnol Bioeng. 2000 Apr 5;68(1):84-91. doi: 10.1002/(sici)1097-0290(20000405)68:1<84::aid-bit10>3.0.co;2-5.

Abstract

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.

MeSH terms

  • Acylation
  • Biotechnology / methods*
  • Candida / metabolism
  • Carcinogens / metabolism
  • Esterases / metabolism*
  • Hydrazines / metabolism
  • Hydroxylamine / metabolism
  • Lipase / metabolism*
  • Nitrogen / metabolism*
  • Solvents
  • Water

Substances

  • Carcinogens
  • Hydrazines
  • Solvents
  • Water
  • hydrazine
  • Hydroxylamine
  • Esterases
  • Lipase
  • Nitrogen