Structural and catalytic aspects of cutinase in w/o microemulsions

Papadimitriou, V; Xenakis, A; Cazianis, CT; Kolisis, FN

dc.contributor.author	Papadimitriou, V	en
dc.contributor.author	Xenakis, A	en
dc.contributor.author	Cazianis, CT	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T01:13:25Z
dc.date.available	2014-03-01T01:13:25Z
dc.date.issued	1997	en
dc.identifier.issn	0303-402X	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12461
dc.subject	AOT	en
dc.subject	Electron Paramagnetic Resonance, EPR	en
dc.subject	Esterification	en
dc.subject	Lipase	en
dc.subject	Microemulsions	en
dc.subject	Reverse micelles	en
dc.subject.classification	Chemistry, Physical	en
dc.subject.classification	Polymer Science	en
dc.subject.other	IN-OIL MICROEMULSIONS	en
dc.subject.other	REVERSE MICELLES	en
dc.subject.other	ALPHA-CHYMOTRYPSIN	en
dc.subject.other	ESTERIFICATION REACTIONS	en
dc.subject.other	RECOMBINANT CUTINASE	en
dc.subject.other	LIPOLYTIC ENZYME	en
dc.subject.other	FUSARIUM-SOLANI	en
dc.subject.other	ACTIVE-SITE	en
dc.subject.other	LIPASE	en
dc.subject.other	STABILITY	en
dc.title	Structural and catalytic aspects of cutinase in w/o microemulsions	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/s003960050126	en
heal.identifier.secondary	http://dx.doi.org/10.1007/s003960050126	en
heal.language	English	en
heal.publicationDate	1997	en
heal.abstract	Structural and catalytic properties of cutinase were studied in bis(2-ethylhexyl) sodium sulfosuccinate (AOT)-isooctane microemulsion systems. The effect of the water content of the microemulsions on the cutinase activity on an esterification reaction of lauric acid with pentanol showed that cutinase followed a bell-shaped profile presenting a maximum at w(o) = 9, with w(o) = [H2O]/[AOT]. Kinetic studies allowed the determination of the apparent parameters K-m and V-max. Electron paramagnetic resonance (EPR) spectroscopy studies of active site labeled cutinase in microemulsions with varying w(o) values showed that in all microemulsions, the mobility of the label is higher than in the aqueous solution. Furthermore, it was found that the maximum of the enzyme activity did not correspond to a reduced active site mobility. Up to w(o) = 9 there was an increase of both activity and active site mobility. As the water content of the system became higher, the mobility of the bound spin label further increased whereas the enzymatic activity dropped considerably.	en
heal.publisher	DR DIETRICH STEINKOPFF VERLAG	en
heal.journalName	Colloid and Polymer Science	en
dc.identifier.doi	10.1007/s003960050126	en
dc.identifier.isi	ISI:A1997XU16500001	en
dc.identifier.volume	275	en
dc.identifier.issue	7	en
dc.identifier.spage	609	en
dc.identifier.epage	616	en