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dc.contributor.authorFlaschel, Erwin
dc.contributor.authorRenken, Albert
dc.date.accessioned2024-03-27T09:41:16Z
dc.date.available2024-03-27T09:41:16Z
dc.date.issued1991
dc.date.submitted2024-03-27
dc.identifier.citationLipases : structure, mechanism and genetic engineering, 349 - 352en_US
dc.identifier.isbn156081165X
dc.identifier.isbn3527283323
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623737
dc.description.abstractNew data are presented for the reaction behaviour of the C. rugosalipase in the presence of soluble substrates. The expected interpretation in terms of the formation of a dimeric species ofthe enzyme has found a rival model in the adsorption of the lipase on the surface of the reactor made of glass.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 16en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleTHE BEHAVIOUR OF THE CANDIDA RUGOSALIPASEIN THE PRESENCE OF SOLUBLE SUBSTRATESen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentInstitut de génie chimique, Ecole Polytechnique Fédérale de Lausanne EPFL-Ecublens, CH-1015 Lausanne, Switzerland; Arbeitsgruppe Fermentationstechnik, Technische Fakultät, Universität Bielefeld P.O.Box 6840, D-4800Bielefeld 1, Germanyen_US
dc.identifier.journalLipases : structure, mechanism and genetic engineering, 1991en_US
refterms.dateFOA2024-03-27T09:41:17Z


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