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Título

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

AutorPessela, Benevides C. ; Fernández-Lorente, Gloria ; Guisán, José Manuel ; Guimarâes, L. H. S.
Palabras claveTannin acyl hydrolase
Tannase
Emericela
Propyl gallate
Enzyme immobilization
Fecha de publicación2013
EditorSpringer
CitaciónBiotechnology Letters 35(4): 591-598 (2013)
ResumenThe 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.
URIhttp://hdl.handle.net/10261/126730
DOI10.1007/s10529-012-1111-4
Identificadoresdoi: 10.1007/s10529-012-1111-4
issn: 0141-5492
e-issn: 1573-6776
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