LIPASES IN REVERSE MICELLES

Walde, Peter; Luisi, Pier Luigi

dc.contributor.author	Walde, Peter
dc.contributor.author	Luisi, Pier Luigi
dc.date.accessioned	2024-03-20T09:17:04Z
dc.date.available	2024-03-20T09:17:04Z
dc.date.issued	1991
dc.date.submitted	2024-03-20
dc.identifier.citation	Lipases : structure, mechanism and genetic engineering, 155 - 158	en_US
dc.identifier.isbn	156081165X
dc.identifier.isbn	3527283323
dc.identifier.issn	0930-4320
dc.identifier.uri	http://hdl.handle.net/10033/623711
dc.description.abstract	Two independent spectroscopic methods have been developed to assay lipases continuously with triacylglycerol substrates in a reverse micellar solution. With the two methods, a simple and unique possibility is offered to study the kinetics and the specificity of lipases, embedded in a system which possibly mimics the biologically relevant environment of lipolytic enzymes. Preliminary activity data are presented for the colipase dependent human pancreatic lipase in reverse micelles, and we have started to investigate the conformational behavior of this enzyme by means of circular dichroism and fluorescence spectroscopy.	en_US
dc.language.iso	en	en_US
dc.publisher	GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig	en_US
dc.relation.ispartofseries	GBF monographs ; Volume 16	en_US
dc.rights	Attribution-NonCommercial-ShareAlike 4.0 International	*
dc.rights.uri	http://creativecommons.org/licenses/by-nc-sa/4.0/	*
dc.title	LIPASES IN REVERSE MICELLES	en_US
dc.type	Book chapter	en_US
dc.type	conference paper	en_US
dc.contributor.department	Institut für Polymere, Eidgenössische Technische Hochschule, Zürich (Switzerland)	en_US
dc.identifier.journal	Lipases : structure, mechanism and genetic engineering, 1991	en_US
refterms.dateFOA	2024-03-20T09:17:05Z