dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorAzevedo Carvalho, Ana Flavia
dc.creatorBoscolo, Mauricio
dc.creatorda Silva, Roberto
dc.creatorFerreira, Henrique
dc.creatorGomes, Eleni
dc.date2014-05-20T14:00:48Z
dc.date2016-10-25T17:08:11Z
dc.date2014-05-20T14:00:48Z
dc.date2016-10-25T17:08:11Z
dc.date2010-08-01
dc.date.accessioned2017-04-05T21:23:50Z
dc.date.available2017-04-05T21:23:50Z
dc.identifierJournal of Microbiology. Seoul: Microbiological Society Korea, v. 48, n. 4, p. 452-459, 2010.
dc.identifier1225-8873
dc.identifierhttp://hdl.handle.net/11449/21476
dc.identifierhttp://acervodigital.unesp.br/handle/11449/21476
dc.identifier10.1007/s12275-010-9319-2
dc.identifierWOS:000281516800007
dc.identifierhttp://dx.doi.org/10.1007/s12275-010-9319-2
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867036
dc.descriptionAn alpha-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at 70 degrees C. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and 60 C. In the presence of ions Na(+), Ba(2+), Co(2+), Ni(2+), Mg(2+), Mn(2+), Al(3+), Zn(2+), Ca(2+) this enzyme maintained 90-105% of its maximum activity and was inhibited by Cr(3+), Ag(+), and Hg(2+). The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and alpha-PNPG. The K(m) measured for the a-glucosidase was 0.07 mu M, with a V(max) of 318.0 mu mol/min/mg.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherMicrobiological Society Korea
dc.relationJournal of Microbiology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectalpha-glucosidase
dc.subjectT. aurantiacus
dc.subjecttermostable enzyme
dc.subjecttransglycosylation reaction
dc.subjectPurification
dc.titlePurification and Characterization of the alpha-Glucosidase Produced by Thermophilic Fungus Thermoascus aurantiacus CBMAI 756
dc.typeOtro


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