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Growth of Candida boidinii in a methanol-limited continuous culture and the formation of methanol-degrading enzymes

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dc.contributor.author Aggelis, G en
dc.contributor.author Fakas, S en
dc.contributor.author Melissis, S en
dc.contributor.author Clonis, YD en
dc.date.accessioned 2014-06-06T06:44:02Z
dc.date.available 2014-06-06T06:44:02Z
dc.date.issued 1999 en
dc.identifier.issn 0168-1656 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/1642
dc.subject Candida boidinii en
dc.subject methanol en
dc.subject methanol oxidase en
dc.subject formaldehyde dehydrogenase en
dc.subject formate dehydrogenase en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other FORMALDEHYDE DEHYDROGENASE en
dc.subject.other YEAST en
dc.subject.other OPTIMIZATION en
dc.subject.other ASSIMILATION en
dc.subject.other PURIFICATION en
dc.subject.other METABOLISM en
dc.subject.other OXIDASE en
dc.title Growth of Candida boidinii in a methanol-limited continuous culture and the formation of methanol-degrading enzymes en
heal.type journalArticle en
heal.language English en
heal.publicationDate 1999 en
heal.abstract The growth of Candida boidinii was studied in a methanol-limited continuous culture showing a linear decrease of dry cell yield with increase of the dilution rate, probably due to an overcapacity of the micro-organism to oxidise methanol. Using a modified Monod equation, the growth parameters were calculated as follows: mu = 0.152 h(-1), Y-max = 0.36 g g(-1), K-s = 1.318 g l(-1) and m(s) = 0.028 g g(-1) h(-1). The activity of methanol oxidase, formaldehyde dehydrogenase and formate dehydrogenase increased in the cell free extract with the decrease of the dilution rate from 0.144 to 0.019 h(-1). Moreover, the increase of specific activity of methanol oxidase and formate dehydrogenase was greater than that of formaldehyde dehydrogenase, probably due to the different affinity of the enzymes for their substrate. These results are important for the regulation of the rate of enzyme synthesis: the rates of specific synthesis for methanol oxidase and formate dehydrogenase are less affected by the shift of the dilution rate, whereas the rate of the specific synthesis for formaldehyde dehydrogenase is strongly dependent on the dilution rate. The maximum productivity of the enzymes was predicted to be 8.74, 92.2 and 15.14 U l(-1) h(-1) at dilution rates of 0.114, 0.111 and 0.105 h(-1) for methanol oxidase, formaldehyde dehydrogenase and formate dehydrogenase, respectively. (C) 1999 Elsevier Science B.V. All rights reserved. en
heal.publisher ELSEVIER SCIENCE BV en
heal.journalName JOURNAL OF BIOTECHNOLOGY en
dc.identifier.issue 1-2 en
dc.identifier.volume 72 en
dc.identifier.isi ISI:000081199300012 en
dc.identifier.spage 127 en
dc.identifier.epage 139 en


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