Acylation of glucose catalysed by lipases in supercritical carbon dioxide

Tsitsimpikou, C; Stamatis, H; Sereti, V; Daflos, H; Kolisis, FN

dc.contributor.author	Tsitsimpikou, C	en
dc.contributor.author	Stamatis, H	en
dc.contributor.author	Sereti, V	en
dc.contributor.author	Daflos, H	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T01:13:33Z
dc.date.available	2014-03-01T01:13:33Z
dc.date.issued	1998	en
dc.identifier.issn	0268-2575	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12560
dc.subject	Glucose acylation	en
dc.subject	Lipase	en
dc.subject	Supercritical carbon dioxide	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Chemistry, Multidisciplinary	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	carbon dioxide	en
dc.subject.other	glucose	en
dc.subject.other	lauric acid	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	water	en
dc.subject.other	acylation	en
dc.subject.other	article	en
dc.subject.other	candida	en
dc.subject.other	catalyst	en
dc.subject.other	chemical reaction kinetics	en
dc.subject.other	enzyme activity	en
dc.subject.other	mucor	en
dc.subject.other	Candida antarctica	en
dc.subject.other	Candida rugosa	en
dc.subject.other	Mucor miehei	en
dc.subject.other	Acylation	en
dc.subject.other	Carbon dioxide	en
dc.subject.other	Catalysis	en
dc.subject.other	Catalyst activity	en
dc.subject.other	Composition effects	en
dc.subject.other	Enzymes	en
dc.subject.other	Organic acids	en
dc.subject.other	Organic solvents	en
dc.subject.other	Reaction kinetics	en
dc.subject.other	Thermal effects	en
dc.subject.other	Thermodynamic stability	en
dc.subject.other	Lipase	en
dc.subject.other	Supercritical carbon dioxide	en
dc.subject.other	Glucose	en
dc.title	Acylation of glucose catalysed by lipases in supercritical carbon dioxide	en
heal.type	journalArticle	en
heal.identifier.primary	10.1002/(SICI)1097-4660(199804)71:4<309::AID-JCTB859>3.0.CO;2-L	en
heal.identifier.secondary	http://dx.doi.org/10.1002/(SICI)1097-4660(199804)71:4<309::AID-JCTB859>3.0.CO;2-L	en
heal.language	English	en
heal.publicationDate	1998	en
heal.abstract	The acylation of glucose with lauric acid in a reaction catalysed by two Candida lipases and a Mucor miehei lipase in supercritical carbon dioxide (SCCO2) was investigated. A linear dependence of the reaction rate on enzyme concentration was observed. Studies on the effect of temperature on enzyme activity showed that Candida antarctica lipase remains stable at temperatures as high as 70 degrees C. Non-immobilised Candida rugosa lipase was found to have a temperature optimum at 60 degrees C. The acylation reaction rate depended on the initial water activity of both substrates and enzyme; the optimum was 0.75 for Candida antarctica lipase, 0.53 for Candida rugosa lipase, and between 0.3 and 0.5 for Mucor miehei lipase. Candida rugosa lipase was most active at a molar ratio of sugar:acyl donor of 1 : 3, while the optimum ratio was found to increase to 1 : 6 when the reaction was catalysed by Candida antarctica and Mucor miehei lipases. (C) 1998 SCI.	en
heal.publisher	JOHN WILEY & SONS LTD	en
heal.journalName	Journal of Chemical Technology and Biotechnology	en
dc.identifier.doi	10.1002/(SICI)1097-4660(199804)71:4<309::AID-JCTB859>3.0.CO;2-L	en
dc.identifier.isi	ISI:000072951400005	en
dc.identifier.volume	71	en
dc.identifier.issue	4	en
dc.identifier.spage	309	en
dc.identifier.epage	314	en