Lipase activity enhancement by SC-CO2 treatment

Hlavsova, K; Wimmer, Z; Xanthakis, E; Bernasek, P; Sovova, H; Zarevucka, M

dc.contributor.author	Hlavsova, K	en
dc.contributor.author	Wimmer, Z	en
dc.contributor.author	Xanthakis, E	en
dc.contributor.author	Bernasek, P	en
dc.contributor.author	Sovova, H	en
dc.contributor.author	Zarevucka, M	en
dc.date.accessioned	2014-03-01T01:28:43Z
dc.date.available	2014-03-01T01:28:43Z
dc.date.issued	2008	en
dc.identifier.issn	0932-0776	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/18941
dc.relation.uri	http://www.scopus.com/inward/record.url?eid=2-s2.0-46949104460&partnerID=40&md5=e80d944a1f30df495379afda1e37a08d	en
dc.subject	Enantioselectivity	en
dc.subject	Lipase activity	en
dc.subject	Supercritical carbon dioxide	en
dc.subject.classification	Chemistry, Inorganic & Nuclear	en
dc.subject.classification	Chemistry, Organic	en
dc.subject.other	SUPERCRITICAL CARBON-DIOXIDE	en
dc.subject.other	PORCINE PANCREATIC LIPASE	en
dc.subject.other	HYDROLASES	en
dc.subject.other	CO2	en
dc.subject.other	BIOCATALYSIS	en
dc.subject.other	HYDROLYSIS	en
dc.subject.other	STABILITY	en
dc.subject.other	REACTOR	en
dc.subject.other	FLUIDS	en
dc.title	Lipase activity enhancement by SC-CO2 treatment	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	2008	en
heal.abstract	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 frani-isomers of 2-(4-methoxybenzyl) cyclIohexyl acetates. Satisfactory reaction yields (40 %) and excellent enantiomeric purity of the products (E = 472) were obtained when hydrolysis of the frans-isomer of 2-(4-methoxybenzyl)cyclohexyl acetate was catalyzed by Lipozyme® treated with SC-CO2. © 2008 Verlag der Zeitschrift für Naturforschung, Tübingen.	en
heal.publisher	VERLAG Z NATURFORSCH	en
heal.journalName	Zeitschrift fur Naturforschung - Section B Journal of Chemical Sciences	en
dc.identifier.isi	ISI:000256944000028	en
dc.identifier.volume	63	en
dc.identifier.issue	6	en
dc.identifier.spage	779	en
dc.identifier.epage	784	en