Pseudomonas cepacia lipase: esterification reactions in AOT microemulsion systems

Stamatis, H; Xenakis, A; Bornscheuer, U; Scheper, T; Menge, U; Kolisis, FN

dc.contributor.author	Stamatis, H	en
dc.contributor.author	Xenakis, A	en
dc.contributor.author	Bornscheuer, U	en
dc.contributor.author	Scheper, T	en
dc.contributor.author	Menge, U	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T01:09:31Z
dc.date.available	2014-03-01T01:09:31Z
dc.date.issued	1993	en
dc.identifier.issn	0141-5492	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/11049
dc.subject	Enzyme	en
dc.subject	Enzyme Activity	en
dc.subject	Fatty Acid	en
dc.subject	Water Content	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	alkanol	en
dc.subject.other	fatty acid	en
dc.subject.other	octanoic acid	en
dc.subject.other	palmitic acid	en
dc.subject.other	propanol	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	article	en
dc.subject.other	burkholderia cepacia	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme purification	en
dc.subject.other	enzyme specificity	en
dc.subject.other	esterification	en
dc.subject.other	nonhuman	en
dc.subject.other	ph	en
dc.subject.other	time	en
dc.subject.other	water content	en
dc.title	Pseudomonas cepacia lipase: esterification reactions in AOT microemulsion systems	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/BF01080143	en
heal.identifier.secondary	http://dx.doi.org/10.1007/BF01080143	en
heal.language	English	en
heal.publicationDate	1993	en
heal.abstract	The activity of purified Pseudomonas cepacia lipase has been investigated in esterification reactions of various aliphatic alcohols with natural fatty acids. The reactions were carried out in microemulsions formed in isooctane by bis(2ethylhexyl)sulfosuccinate sodium salt (AOT). The optima pH, T and water content (w(o)) for the enzyme activity in this type of microemulsions have been determined. Studies on the effect of various fatty acids and alcohols on the enzyme specificity have shown a preference of this lipase for palmitic and caprylic acid as well as for propanol, while reactions involving cyclic alcohols can not be catalyzed at all. The differences on the behavior of this lipase as compared to other lipases studied in microemulsion systems as well as in other systems are discussed.	en
heal.publisher	CHAPMAN HALL LTD	en
heal.journalName	Biotechnology Letters	en
dc.identifier.doi	10.1007/BF01080143	en
dc.identifier.isi	ISI:A1993LQ25400008	en
dc.identifier.volume	15	en
dc.identifier.issue	7	en
dc.identifier.spage	703	en
dc.identifier.epage	708	en