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Production and characterization of extracellular lipase from Calvatia gigantea

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dc.contributor.author Christakopoulos, P en
dc.contributor.author Tzia, C en
dc.contributor.author Kekos, D en
dc.contributor.author Macris, BJ en
dc.date.accessioned 2014-03-01T01:09:00Z
dc.date.available 2014-03-01T01:09:00Z
dc.date.issued 1992 en
dc.identifier.issn 0175-7598 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/10795
dc.subject Culture Medium en
dc.subject Enzyme en
dc.subject Kinetics en
dc.subject Nitrogen en
dc.subject Number of Factors en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other triacylglycerol lipase en
dc.subject.other article en
dc.subject.other biosynthesis en
dc.subject.other enzyme synthesis en
dc.subject.other fungus en
dc.title Production and characterization of extracellular lipase from Calvatia gigantea en
heal.type journalArticle en
heal.identifier.primary 10.1007/BF00174467 en
heal.identifier.secondary http://dx.doi.org/10.1007/BF00174467 en
heal.language English en
heal.publicationDate 1992 en
heal.abstract A number of factors affecting production of extracellular lipase by the edible fungus Calvatia gigantea were investigated. Consecutive optimization of carbon and nitrogen sources, initial pH of culture medium and growth temperature resulted in an increase in lipase activity of 87%. Under optimum conditions, activities as high as 22.4 units ml-1 of culture medium were obtained, competing favourably with most activities reported for other lipase hyperproducing microorganisms. The enzyme was optimally active at pH 7.0 and 300-degrees-C and had, at optimum pH, half-lives of 75.7 and 22.9 min at 45 and 55-degrees-C. Both high activity and kinetic characteristics of the enzyme make this process worthy of further investigation. en
heal.publisher SPRINGER VERLAG en
heal.journalName Applied Microbiology and Biotechnology en
dc.identifier.doi 10.1007/BF00174467 en
dc.identifier.isi ISI:A1992KB40600011 en
dc.identifier.volume 38 en
dc.identifier.issue 2 en
dc.identifier.spage 194 en
dc.identifier.epage 197 en


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