Lipase Activity Enhancement by SC-CO 2 Treatment

• Published in: Zeitschrift für Naturforschung B
• Format: Article in Journal/Newspaper
• Language: English
• Published: Walter de Gruyter GmbH 2008
• Subjects: antartic*
• Online Access: http://dx.doi.org/10.1515/znb-2008-0628; https://www.degruyter.com/view/journals/znb/63/6/article-p779.xml; https://www.degruyter.com/document/doi/10.1515/znb-2008-0628/xml; https://www.degruyter.com/document/doi/10.1515/znb-2008-0628/pdf

The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was studied after using them as biocatalysts of blackcurrant oil hydrolysis under SC-CO₂ conditions. The reaction was performed at 40 °C and 15 MPa in a continuous-flow reactor. Increased relative activity of all used lipases after the hydrolytic reaction was observed. The most remarkable increase in the activity was noted for the lipase from Rhizopus arrhizus which was increased by more than 50 times. The highest activity was shown by Lipozyme® , lipase from Mucor miehei immobilized on macroporous resin. Both treated and untreated Lipozyme® were used as biocatalysts in hydrolytic resolution of the racemic cis- or trans-isomers of 2-(4-methoxybenzyl)cyclohexyl acetates. Satisfactory reaction yields (40 %) and excellent enantiomeric purity of the products (E = 472) were obtained when hydrolysis of the trans-isomer of 2-(4-methoxybenzyl)cyclohexyl acetate was catalyzed by Lipozyme® treated with SC-CO₂.