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dc.contributor.authorLang, S.
dc.contributor.authorKatsiwela, E.
dc.contributor.authorKleppe, F.
dc.contributor.authorWagner, Fritz
dc.date.accessioned2024-03-27T09:53:57Z
dc.date.available2024-03-27T09:53:57Z
dc.date.issued1991
dc.date.submitted2024-03-27
dc.identifier.citationLipases : structure, mechanism and genetic engineering, 361 - 364en_US
dc.identifier.isbn156081165X
dc.identifier.isbn3527283323
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623739
dc.description.abstractThe crude lipase preparation of Ustilago maydis ATCC 14826 (after growth on coconut oil) was studied with respect to hydrolysis and esterification potential, resp., as well as to purification of lipolytic enzymes. Concerning substrate specifity (hydrolysis) among triglycerides short chain substances were cleaved to an higher extent than long chain or unsaturated compounds. Obvious inhibition of lipase activity was observed when additional amounts of linoleic or linolenic acid were used during hydrolysis of coconut oil. After Amberlite XAD-2 immobilization and transfer into n-hexane the wax ester synthesis potential was confirmed. The purification of crude lipase preparation by chromatographic methods led to two lipolytic enzymes.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.titleUSTILAGO MAYDIS LIPOLYTIC ENZYMES: CHARACTERIZATION AND PARTIAL PURIFICATIONen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentInstitute of Biochemistry and Biotechnology, Technical University, D-3300 Braunschweig, West-Germanyen_US
dc.identifier.journalLipases : structure, mechanism and genetic engineering, 1991en_US
refterms.dateFOA2024-03-27T09:53:59Z


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Attribution-NonCommercial-ShareAlike 4.0 International
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