dc.creatorMasui, Douglas Chodi
dc.creatorZimbardi, Ana Lucia Ribeiro Latorre
dc.creatorSouza, Flavio Henrique Moreira de
dc.creatorGuimarães, Luis Henrique Souza
dc.creatorFurriel, Rosa dos Prazeres Melo
dc.creatorJorge, Joao Atilio
dc.date.accessioned2013-11-04T14:33:42Z
dc.date.accessioned2018-07-04T16:15:51Z
dc.date.available2013-11-04T14:33:42Z
dc.date.available2018-07-04T16:15:51Z
dc.date.created2013-11-04T14:33:42Z
dc.date.issued2012
dc.identifierWORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, NEW YORK, v. 28, n. 8, supl. 1, Part 1, pp. 2689-2701, AUG, 2012
dc.identifier0959-3993
dc.identifierhttp://www.producao.usp.br/handle/BDPI/40869
dc.identifier10.1007/s11274-012-1079-1
dc.identifierhttp://dx.doi.org/10.1007/s11274-012-1079-1
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1633583
dc.description.abstractHumicola brevis var. thermoidea cultivated under solid state fermentation in wheat bran and water (1:2 w/v) was a good producer of beta-glucosidase and xylanase. After optimization using response surface methodology the level of xylanase reached 5,791.2 +/- A 411.2 U g(-1), while beta-glucosidase production was increased about 2.6-fold, reaching 20.7 +/- A 1.5 U g(-1). Cellulase levels were negligible. Biochemical characterization of H. brevis beta-glucosidase and xylanase activities showed that they were stable in a wide pH range. Optimum pH for beta-glucosidase and xylanase activities were 5.0 and 5.5, respectively, but the xylanase showed 80 % of maximal activity when assayed at pH 8.0. Both enzymes presented high thermal stability. The beta-glucosidase maintained about 95 % of its activity after 26 h in water at 55 A degrees C, with half-lives of 15.7 h at 60 A degrees C and 5.1 h at 65 A degrees C. The presence of xylose during heat treatment at 65 A degrees C protected beta-glucosidase against thermal inactivation. Xylanase maintained about 80 % of its activity after 200 h in water at 60 A degrees C. Xylose stimulated beta-glucosidase activity up to 1.7-fold, at 200 mmol L-1. The notable features of both xylanase and beta-glucosidase suggest that H. brevis crude culture extract may be useful to compose efficient enzymatic cocktails for lignocellulosic materials treatment or paper pulp biobleaching.
dc.languageeng
dc.publisherSPRINGER
dc.publisherNEW YORK
dc.relationWORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
dc.rightsCopyright SPRINGER
dc.rightsrestrictedAccess
dc.subjectBETA-GLUCOSIDASE
dc.subjectTHERMOSTABLE XYLANASE
dc.subjectXYLOSE STIMULATED BETA-GLUCOSIDASE
dc.subjectHUMICOLA BREVIS
dc.subjectTHERMOPHILIC FUNGI
dc.titleProduction of a xylose-stimulated beta-glucosidase and a cellulase-free thermostable xylanase by the thermophilic fungus Humicola brevis var. thermoidea under solid state fermentation
dc.typeArtículos de revistas


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