Studies on localization and regulation of lipase production by Aspergillus niger

Macris, JB; Kourentzi, E; Hatzinikolaou, DG

dc.contributor.author	Macris, JB	en
dc.contributor.author	Kourentzi, E	en
dc.contributor.author	Hatzinikolaou, DG	en
dc.date.accessioned	2014-03-01T01:12:20Z
dc.date.available	2014-03-01T01:12:20Z
dc.date.issued	1996	en
dc.identifier.issn	0032-9592	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12064
dc.subject	Aspergillus Niger	en
dc.subject	Enzyme	en
dc.subject	Fatty Acid	en
dc.subject	Organic Solvent	en
dc.subject	Oleic Acid	en
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	fatty acid	en
dc.subject.other	glucose	en
dc.subject.other	glycerol	en
dc.subject.other	lipid	en
dc.subject.other	oleic acid	en
dc.subject.other	triacylglycerol	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	triolein	en
dc.subject.other	article	en
dc.subject.other	aspergillus niger	en
dc.subject.other	biomass	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme assay	en
dc.subject.other	enzyme localization	en
dc.subject.other	enzyme regulation	en
dc.subject.other	enzyme specificity	en
dc.subject.other	enzyme structure	en
dc.subject.other	enzyme synthesis	en
dc.subject.other	Aspergillus niger	en
dc.title	Studies on localization and regulation of lipase production by Aspergillus niger	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S0032-9592(96)00037-4	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S0032-9592(96)00037-4	en
heal.language	English	en
heal.publicationDate	1996	en
heal.abstract	The lipase from strain BTL of Aspergillus niger was studied. The enzyme, which was mainly extracellular; was produced at elevated activity levels under optimum growth conditions. De novo biosynthesis of lipase occurred only in the presence of lipids and was completely repressed by glucose and glycerol. The reaction products, oleic acid and glycerol, showed differed inhibition patterns during triolein hydrolysis. The enzyme exhibited high specificity towards middle chain triglycerides and was possibly activated by double bonds in the fatty acid chain. It exhibited a marked stability against organic solvents. Copyright (C) 1996 Elsevier Science Ltd.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	Process Biochemistry	en
dc.identifier.doi	10.1016/S0032-9592(96)00037-4	en
dc.identifier.isi	ISI:A1996VJ09200008	en
dc.identifier.volume	31	en
dc.identifier.issue	8	en
dc.identifier.spage	807	en
dc.identifier.epage	812	en