Functional properties of a manganese-activated exo-polygalacturonase produced by a thermotolerant fungus Aspergillus niveus

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dc.contributor.authorMaller, Alexandre
dc.contributor.authorSilva, Tony Marcio da
dc.contributor.authorLima damasio, Andre Ricardo de
dc.contributor.authorHirata, Izaura Yoshico [UNIFESP]
dc.contributor.authorJorge, Joao Atilio
dc.contributor.authorTerenzi, Hector Francisco
dc.contributor.authorTeixeira de Moraes Polizeli, Maria de Lourdes
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:34:40Z
dc.date.available2016-01-24T14:34:40Z
dc.date.issued2013-11-01
dc.description.abstractA thermotolerant fungus identified as Aspergillus niveus was isolated from decomposing materials and it has produced excellent levels of hydrolytic enzymes that degrade plant cell walls. A. niveus germinated faster at 40 A degrees C, presenting protein levels almost twofold higher than at 25 A degrees C. the crude extract of the A. niveus culture was purified by diethylaminoethyl (DEAE)-cellulose, followed by Biogel P-100 column. Polygalacturonase (PG) is a glycoprotein with 37.7 % carbohydrate, molecular mass of 102.6 kDa, and isoelectric point of 5.4. the optimum temperature and pH were 50 A degrees C and 4.0-6.5, respectively. the enzyme was stable at pH 3.0 to 9.0 for 24 h. the DEAE-cellulose derivative was about sixfold more stable at 60 A degrees C than the free enzyme. Moreover, the monoaminoethyl-N-aminoethyl-agarose derivative was tenfold more stable than the free enzyme. PG was 232 % activated by Mn2+. the hydrolysis product of sodium polypectate corresponded at monogalacturonic acid, which classifies the enzyme as an exo-PG. the K (m), V (max), K (cat), and K (cat)/K (m) values were 6.7 mg/ml, 230 U/mg, 393.3/s, and 58.7 mg/ml/s, respectively. the N-terminal amino acid sequence presented 80 % identity with PglB1, PglA2, and PglA3 putative exo-PG of Aspergillus fumigatus and an exo-PG Neosartorya fischeri.en
dc.description.affiliationUniv São Paulo, Dept Bioquim & Imunol, Fac Med & Imunol Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Dept Biol, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, Ribeirao Preto, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, Ribeirao Preto, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent615-621
dc.identifierhttp://dx.doi.org/10.1007/s12223-013-0249-3
dc.identifier.citationFolia Microbiologica. Dordrecht: Springer, v. 58, n. 6, p. 615-621, 2013.
dc.identifier.doi10.1007/s12223-013-0249-3
dc.identifier.issn0015-5632
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/36932
dc.identifier.wosWOS:000324835100025
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofFolia Microbiologica
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.titleFunctional properties of a manganese-activated exo-polygalacturonase produced by a thermotolerant fungus Aspergillus niveusen
dc.typeinfo:eu-repo/semantics/article
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