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Optimizing production of extracellular lipase from rhodotorula glutinis

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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


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