Production and partial characterisation of extracellular lipase from Aspergillus niger

Hatzinikolaou, DG; Macris, JB; Christakopoulos, P; Kekos, D; Kolisis, FN; Fountoukidis, G

dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Macris, JB	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Kolisis, FN	en
dc.contributor.author	Fountoukidis, G	en
dc.date.accessioned	2014-03-01T01:12:11Z
dc.date.available	2014-03-01T01:12:11Z
dc.date.issued	1996	en
dc.identifier.issn	01415492	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/12005
dc.subject	Aspergillus Niger	en
dc.subject	Enzyme	en
dc.subject	Experimental Design	en
dc.subject	Kinetics	en
dc.subject	Nitrogen	en
dc.subject	Response Surface	en
dc.subject.other	carbon	en
dc.subject.other	nitrogen	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	article	en
dc.subject.other	aspergillus niger	en
dc.subject.other	controlled study	en
dc.subject.other	enzyme activation	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme synthesis	en
dc.subject.other	extracellular space	en
dc.subject.other	nonhuman	en
dc.subject.other	ph	en
dc.subject.other	temperature sensitivity	en
dc.title	Production and partial characterisation of extracellular lipase from Aspergillus niger	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/BF00140201	en
heal.identifier.secondary	http://dx.doi.org/10.1007/BF00140201	en
heal.publicationDate	1996	en
heal.abstract	The production and certain kinetic characteristics of extracellular lipase from Aspergillus niger were investigated. It was possible to substantially enhance the activity of excreted lipase by optimising the interaction between carbon and nitrogen sources applying a two-parameter complete experimental design and response surface analysis. The enzyme was partially purified and a number of kinetic characteristics such as optimum pH and temperature, thermal and pH stability and K(m) were determined and discussed. The elevated levels of lipase activity (40.5 U/ml) found in this work competed favourably with most of those reported for lipase hyperproducing fungi.	en
heal.journalName	Biotechnology Letters	en
dc.identifier.doi	10.1007/BF00140201	en
dc.identifier.volume	18	en
dc.identifier.issue	5	en
dc.identifier.spage	547	en
dc.identifier.epage	552	en