dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-27T11:27:29Z
dc.date.accessioned2022-10-05T18:40:49Z
dc.date.available2014-05-27T11:27:29Z
dc.date.available2022-10-05T18:40:49Z
dc.date.created2014-05-27T11:27:29Z
dc.date.issued2013-01-01
dc.identifierJournal of Molecular Catalysis B: Enzymatic, v. 85-86, p. 126-133.
dc.identifier1381-1177
dc.identifier1873-3158
dc.identifierhttp://hdl.handle.net/11449/74187
dc.identifier10.1016/j.molcatb.2012.09.001
dc.identifierWOS:000312231000018
dc.identifier2-s2.0-84866863408
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3923151
dc.description.abstractTannases have attracted wider attention because of their biotechnological potential, especially enzymes from filamentous fungi and other microorganisms. However, the biodiversity of these microorganisms has been poorly explored, and few strains were identified for tannase production and characterization. This article describes the production, purification and characterization of a glucose- and solvent-tolerant extracellular tannase from Aspergillus phoenicis. High enzymatic levels were obtained in Khanna medium containing tannic acid up to 72 h at 30 °C under 100 rpm. The purified enzyme with 65% of carbohydrate content had an apparent native molecular mass of 218 kDa with subunits of 120 kDa and 93 kDa and was stable at 50 °C for 1 h. Optima of temperature and pH were 60 °C and 5.0-6.5, respectively. The enzyme was not affected significantly by most ions, detergents and organic solvents. While glucose did not affect the tannase activity, the addition of a high concentration of gallic acid did. The Km values were 1.7 mM (tannic acid), 14.3 mM (methyl-gallate) and 0.6 mM (propyl-gallate). The enzyme was able to catalyze the transesterification reaction to produce propyl-gallate. All biochemical properties suggest the biotechnological potential of the glucose- and solvent-tolerant tannase from A. phoenicis. © 2012 Elsevier B.V. All rights reserved.
dc.languageeng
dc.relationJournal of Molecular Catalysis B: Enzymatic
dc.relation0,522
dc.rightsAcesso restrito
dc.sourceScopus
dc.subjectAspergillus
dc.subjectEnzyme characterization
dc.subjectGlucose-tolerant enzyme
dc.subjectOrganic solvent
dc.subjectTannase
dc.subjectAspergillus phoenicis
dc.subjectBiochemical properties
dc.subjectCarbohydrate content
dc.subjectExtracellular
dc.subjectFilamentous fungi
dc.subjectGallic acids
dc.subjectHigh concentration
dc.subjectPurified enzyme
dc.subjectTannic acid
dc.subjectTransesterification reaction
dc.subjectBiodiversity
dc.subjectBiotechnology
dc.subjectCarbohydrates
dc.subjectCharacterization
dc.subjectEnzymes
dc.subjectFlavonoids
dc.subjectMicroorganisms
dc.subjectOrganic solvents
dc.subjectPurification
dc.subjectSoaps (detergents)
dc.subjectSolvents
dc.subjectGlucose
dc.subjectdetergent
dc.subjectgallic acid methyl ester
dc.subjectgallic acid propyl ester
dc.subjectglucose
dc.subjectorganic solvent
dc.subjecttannase
dc.subjecttannin
dc.subjectcarbohydrate analysis
dc.subjectcarbon source
dc.subjectcatalysis
dc.subjectconcentration (parameters)
dc.subjectculture medium
dc.subjectenzyme activity
dc.subjectenzyme purification
dc.subjectenzyme synthesis
dc.subjecthydrolysis
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpH
dc.subjectthermostability
dc.subjecttransesterification
dc.subjectFungi
dc.titleCharacterization of a glucose- and solvent-tolerant extracellular tannase from Aspergillus phoenicis
dc.typeArtigo


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