F. Molinari et al., Mycelium-bound carboxylesterase from Aspergillus oryzae: an efficient catalyst for acetylation in organic solvent, ENZYME MICR, 27(8), 2000, pp. 626-630
Dry mycelium of a strain of Aspergillus oryzae efficiently catalyzed the es
terification between free acetic acid and primary alcohols (geraniol and et
hanol) in organic solvent. The growth conditions to obtain high activity of
mycelium-bound enzymes were firstly evaluated. A medium containing Tween 8
0 as carbon source furnished mycelium with the highest activity in the hydr
olysis of alpha-naphthyl esters (alpha-N-acetate, butyrate, caprylate). Dry
mycelium was employed to select suited conditions for an efficient acetyla
tion of ethanol and geraniol in heptane. Maximum productions were obtained
using 30 gl(-1) of lyophilized cells: 12.4 gl(-1) of geranyl acetate were p
roduced at 80 degrees C starting from 75 mM geraniol and acetic acid (84% m
olar conversion) and 4.1 gl(-1) of ethyl acetate at 50 degrees C from 50 mM
ethanol and acetic acid (94% molar conversion) after 24 h. The stability o
f the mycelium-bound carboxylesterases are notable since only 10-30% loss o
f activity was observed after 14 days at temperatures between 30 and 50 deg
rees C. (C) 2000 Elsevier Science Inc. All rights reserved.