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Lipase and esterase‐catalyzed acylation of hetero‐substituted nitrogen nucleophiles in water and organic solvents
Author(s) -
Hacking Michiel A. P. J.,
Akkus Hüseyin,
van Rantwijk Fred,
Sheldon Roger A.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(20000405)68:1<84::aid-bit10>3.0.co;2-5
Subject(s) - chemistry , nucleophile , lipase , acylation , catalysis , organic chemistry , candida antarctica , hydroxylamine , esterase , solvent , yield (engineering) , hydrazine (antidepressant) , enzyme , chromatography , materials science , metallurgy
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°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. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 68: 84–91, 2000.