Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor

The behaviour of an ultrafiltration membrane reactor (UFMR) (60 cm 3 of reactor volume) for the optical resolution of dl-butyrine catalysed by l-aminoacylase was studied, and the influence of substrate concentration (15–25 mmol dm −3 in N-acetyl- l-butyrine), temperature (30–50 °C) and the presence...

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Bibliographic Details
Published in:Enzyme and microbial technology 2004-08, Vol.35 (2), p.261-266
Main Authors: Bódalo, Antonio, Gómez, José L, Gómez, Elisa, Máximo, M.Fuensanta, Montiel, M.Claudia
Format: Article
Language:English
Subjects:
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
dl-Butyrine resolution
Fundamental and applied biological sciences. Psychology
l-Aminoacylase deactivation
Methods. Procedures. Technologies
N-Acetyl- dl-butyrine
Ultrafiltration membrane reactor
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Summary:The behaviour of an ultrafiltration membrane reactor (UFMR) (60 cm 3 of reactor volume) for the optical resolution of dl-butyrine catalysed by l-aminoacylase was studied, and the influence of substrate concentration (15–25 mmol dm −3 in N-acetyl- l-butyrine), temperature (30–50 °C) and the presence of CoCl 2 (0.5 mmol dm −3) on enzyme deactivation was analysed. Adsorption studies with polysulphone and regenerated cellulose membranes (30 cm 2 of filtration surface), as well as deactivation studies in the reaction conditions, were carried out to determine the causes of deactivation. A single-step deactivation scheme is proposed, and it was shown that this first-order model adequately describes enzyme deactivation. The dependence of K d on the enzyme concentration points to the enzyme deactivation, which is mainly caused by the adsorption phenomena on the membrane surface.
ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2004.05.003