Thermostable conidial and mycelial alkaline phosphatases from the thermophilic fungus Scytalidium thermophilum

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorGuimaraes, LHS
dc.creatorTerenzi, H. F.
dc.creatorJorge, J. A.
dc.creatorPolizeli, MLTM
dc.date2014-05-20T15:19:54Z
dc.date2016-10-25T17:52:53Z
dc.date2014-05-20T15:19:54Z
dc.date2016-10-25T17:52:53Z
dc.date2001-10-01
dc.date.accessioned2017-04-05T23:22:47Z
dc.date.available2017-04-05T23:22:47Z
dc.identifierJournal of Industrial Microbiology & Biotechnology. New York: Nature America Inc., v. 27, n. 4, p. 265-270, 2001.
dc.identifier1367-5435
dc.identifierhttp://hdl.handle.net/11449/31291
dc.identifierhttp://acervodigital.unesp.br/handle/11449/31291
dc.identifier10.1038/sj.jim.7000196
dc.identifierWOS:000171716700013
dc.identifierhttp://dx.doi.org/10.1038/sj.jim.7000196
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/875869
dc.descriptionAn extracellular (conidial) and an intracellular (mycelial) alkaline phosphatase from the thermophilic fungus Scytalidium thermophilum were purified by DEAE-cellulose and Concanavalin A-Sepharose chromatography. These enzymes showed allosteric behavior either in the presence or absence of MgCl2, BaCl2, CuCl2, and ZnCl2. All of these ions increased the maximal velocity of both enzymes. The molecular masses of the conidial and mycelial enzymes, estimated by gel filtration, were 162 and 132 kDa, respectively. Both proteins migrated on SDS-PAGE as a single polypeptide of 63 and 58.5 kDa, respectively, suggesting that these enzymes were dimers of identical subunits. The best substrate for the conidial and mycelial phosphatases was p-nitrophenylphosphate, but,beta -glycerophosphate and other phosphorylated compounds also served as substrates. The optimum pH for the conidial and mycelial alkaline phosphatases was 10.0 and 9.5 in the presence of AMPOL buffer, and their carbohydrate contents were about 54% and 63%, respectively. The optimum temperature was 70-75 degreesC for both activities. The enzymes were fully stable up to 1 h at 60 degreesC. These and other properties suggested that the alkaline phosphatases of S. thermophilum might be suitable for biotechnological applications.
dc.languageeng
dc.publisherNature America Inc
dc.relationJournal of Industrial Microbiology & Biotechnology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectScytalidium thermophilum
dc.subjectalkaline phosphatase
dc.subjectacid phosphatase
dc.subjectthermophilic fungi
dc.titleThermostable conidial and mycelial alkaline phosphatases from the thermophilic fungus Scytalidium thermophilum
dc.typeOtro


Este ítem pertenece a la siguiente institución