Optimizing production of extracellular lipase from rhodotorula glutinis

Papaparaskevas, D; Christakopoulos, P; Kekos, D; Macris, BJ

dc.contributor.author	Papaparaskevas, D	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T01:08:59Z
dc.date.available	2014-03-01T01:08:59Z
dc.date.issued	1992	en
dc.identifier.issn	0141-5492	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/10778
dc.subject	Culture Medium	en
dc.subject	Enzyme	en
dc.subject	Kinetics	en
dc.subject	Nitrogen	en
dc.subject.classification	Biotechnology & Applied Microbiology	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	culture medium	en
dc.subject.other	enzyme activity	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme synthesis	en
dc.subject.other	half life time	en
dc.subject.other	nonhuman	en
dc.subject.other	ph	en
dc.subject.other	rhodotorula	en
dc.subject.other	temperature	en
dc.subject.other	Rhodotorula glutinis	en
dc.title	Optimizing production of extracellular lipase from rhodotorula glutinis	en
heal.type	journalArticle	en
heal.identifier.primary	10.1007/BF01021254	en
heal.identifier.secondary	http://dx.doi.org/10.1007/BF01021254	en
heal.language	English	en
heal.publicationDate	1992	en
heal.abstract	Production of extracellular lipase by Rhodotorula glutinis was substantially enhanced when the type and concentration of carbon and nitrogen source, the initial pH of culture medium and the growth temperature were consecutively optimized. Lipase activity as high as 30.4 U/ml of culture medium was obtained at optimum conditions, comparing favourably with most of the activities reported for other lipase hyperproducing microorganisms. The enzyme was optimally active at pH 7.5 and 35-degrees-C and had, at optimum pH, half-lives of 45 and 11.8 min at 45 and 55-degrees-C respectively. The high activity and kinetic characteristics of the enzyme make this process worthy of further investigation.	en
heal.publisher	CHAPMAN HALL LTD	en
heal.journalName	Biotechnology Letters	en
dc.identifier.doi	10.1007/BF01021254	en
dc.identifier.isi	ISI:A1992HX12200011	en
dc.identifier.volume	14	en
dc.identifier.issue	5	en
dc.identifier.spage	397	en
dc.identifier.epage	402	en