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Characterization of a tannase from Emericela nidulans immobilized on ionic and covalent supports for propyl gallate synthesis

AuthorsPessela, Benevides C. ; Fernández-Lorente, Gloria ; Guisán, José Manuel ; Guimarâes, L. H. S.
KeywordsTannin acyl hydrolase
Propyl gallate
Enzyme immobilization
Issue Date2013
CitationBiotechnology Letters 35(4): 591-598 (2013)
AbstractThe 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.
Identifiersdoi: 10.1007/s10529-012-1111-4
issn: 0141-5492
e-issn: 1573-6776
Appears in Collections:(IFI) Artículos
(ICP) Artículos
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