Gonçalves, Heloísa Bressan [UNESP]Jorge, João AtílioPessela, Benevides CostaLorente, Glória FernandezGuisán, José ManuelGuimarães, Luis Henrique Souza2014-05-272014-05-272013-01-01Biotechnology Letters, v. 35, n. 4, p. 591-598, 2013.0141-54921573-6776http://hdl.handle.net/11449/74130The extracellular tannase from Emericela nidulans was immobilized on different ionic and covalent supports. The derivatives obtained using DEAE-Sepharose and Q-Sepharose were thermally stable from 60 to 75 °C, with a half life (t50) >24 h at 80 °C at pH 5. 0. The glyoxyl-agarose and amino-glyoxyl derivatives showed a thermal stability which was lower than that observed for ionic supports. However, when the stability to pH was considered, the derivatives obtained from covalent supports were more stable than those obtained from ionic supports. DEAE-Sepharose and Q-Sepharose derivatives as well as the free enzyme were stable in 30 and 50 % (v/v) 1-propanol. The CNBr-agarose derivative catalyzed complete tannic acid hydrolysis, whereas the Q-Sepharose derivative catalyzed the transesterification reaction to produce propyl gallate (88 % recovery), which is an important antioxidant. © 2012 Springer Science+Business Media Dordrecht.591-598engEmericelaEnzyme immobilizationPropyl gallateTannaseTannin acyl hydrolase1-propanolExtracellularFree enzymeHalf livesQ-SepharoseTannic acidThermally stableTransesterification reactionCatalysisFlavonoidsThermodynamic stabilitySynthesis (chemical)carboxylesterasegallic acid propyl esterimmobilized enzymetannasetannin derivativechemistryEmericellaenzyme stabilityenzymologymetabolismpHtemperatureCarboxylic Ester HydrolasesEnzyme StabilityEnzymes, ImmobilizedHydrogen-Ion ConcentrationPropyl GallateTanninsTemperatureArtigo10.1007/s10529-012-1111-4WOS:000316081800016Acesso restrito2-s2.0-84874814840