L. Giorno et al., PERFORMANCE OF A BIPHASIC ORGANIC AQUEOUS HOLLOW-FIBER REACTOR USING IMMOBILIZED LIPASE, Journal of chemical technology and biotechnology, 64(4), 1995, pp. 345-352
A biphasic organic/aqueous membrane bioreactor, which combined chemica
l reaction with continuous extraction of product in the aqueous phase,
was investigated. Lipase from Candida cylindracea was used as catalys
t with the hydrolysis of triglycerides, to fatty acids and glycerol, a
s a model-system for studying the optimal operating conditions. Asymme
tric capillary membranes, made of polyamide, were used as support for
the enzyme, which was immobilized into the sponge layer of the membran
e by cross-how filtration. The catalytic behaviour of lipase, both imm
obilized in a hydrophylic membrane and free in solution, was compared.
The effects of pH, temperature and substrate concentration on reactor
performance were studied. The catalytic stability of the immobilized
enzyme was improved compared with the enzyme in solution. The immobili
zed lipase showed no deactivation in an operating period of 16 days wh
ereas lipase in solution gave an 80% decrease in specific activity aft
er 2 days of continuous operation. The specific activity of immobilize
d lipase was significantly influenced by the amount of enzyme loaded i
nto the membranes. The optimal range of immobilized protein was betwee
n 2 and 12 mg cm(-3). The positive results obtained with the model-sys
tem were also confirmed using the biphasic organic/aqueous membrane bi
oreactor in a potential practical application, namely the conversion a
nd separation of one enantiomer from an organic racemic mixture of an
ester.