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Enzymatic resolution of (S)‐(+)‐naproxen in a continuous reactor
Author(s) -
Battistel Ezio,
Bianchi Daniele,
Cesti Pietro,
Pina Carlo
Publication year - 1991
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/bit.260380611
Subject(s) - bioreactor , amberlite , lipase , chemistry , chromatography , naproxen , immobilized enzyme , hydrolysis , substrate (aquarium) , adsorption , triacylglycerol lipase , product inhibition , organic chemistry , enzyme , medicine , oceanography , alternative medicine , non competitive inhibition , pathology , geology
An enzymatic method for the continuous production of (S)−(+)−2−(6‐methoxy‐2‐naphthyl) propionic acid (Naproxen) has been developed. The process consists of a stereoselective hydrolysis of the racemic Naproxen ethoxyethyl ester catalyzed by Candida cylindracea lipase. The reaction has been carried out in a continuous‐flow closed‐loop column bioreactor packed with Amberlite XAD−7, a slightly polor resin on which the lipase has been immobilized by adsorption. Various immobilization conditions as well as the properties of the immobilized lipase have been studied. The performance and the productivity of the bioreactor were evaluated as a function of the critical reaction parameters such as temperature, substrate concentration, and product inhibition. By using a 500‐mL column bioreactor, 1.8 kg of optically pure (S)‐(+)‐Naproxen were produced after 1200 h of continuous operation with a slight loss of the enzymatic activity.