Four commercially available lipases, both free and immobilized, were tested
for their ability to catalyze hydrolysis of blackcurrant (Ribes nigrum) oi
l using two different approaches. The lipase from Mucor miehei was studied
free and immobilized in two different ways. The former series of enzymic re
actions were performed in tap water at 40 degrees C, but the latter series
of enzymic processes were carried out in mixtures of isooctane and phosphat
e buffer (in a typical 2/1 ratio of the components) at 30 degrees C. These
conditions were optimized to increase and/or to maximize the yields of the
products, which were priority targets in this study. A rate of hydrolysis a
nd a selective preference of the hydrolytic enzymes towards fatty acids, wi
th a special focus on enrichment of alpha-linolenic acid and/or gamma-linol
enic acid, were studied. Higher rates of hydrolysis of the blackcurrant oil
in the former series of reactions were observed with the immobilized lipas
e from Pseudomonas cepacia used as biocatalyst. In the latter approach, the
most favorable results of the rate of hydrolysis of the target blackcurran
t oil were achieved with the immobilized lipase from Mucor miehei employed
as biocatalyst. Only three lipases, selected from a series of lipases teste
d during this investigation, displayed specificity towards alpha-linolenic
acid and gamma-linolenic acid, i.e. the immobilized lipase from P. cepacia,
lipase from M. miehei and lipase from P. fluorescens. (C) 2000 Elsevier Sc
ience Inc. All rights reserved.