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Título

Characterization of a bacterial tannase from Streptococcus gallolyticus UCN34 suitable for tannin biodegradation

Autor Jiménez, Natalia ; Barcenilla Moraleda, José Maria; Rivas, Blanca de las ; Muñoz, Rosario
Palabras clave Antioxidant
Gallic acid
Esterase
Tannas
Streptococcus
Hydrolase
Fecha de publicación jul-2014
EditorSpringer
Citación Applied Microbiology and Biotechnology 98(14): 6329-6337 (2014)
ResumenThe gene in the locus GALLO-1609 from Streptococcus gallolyticus UCN34 was cloned and expressed as an active protein in Escherichia coli BL21 (DE3). The protein was named TanSg1 since it shows similarity to bacterial tannases previously described. The recombinant strain produced His-tagged TanSg1 which was purified by affinity chromatography. Purified TanSg1 protein showed tannase activity, having a specific activity of 577 U/mg which is 41 % higher than the activity of Lactobacillus plantarum tannase. Remarkably, TanSg1 displayed optimum catalytic activity at pH 6-8 and 50-70°C and showed high stability over a broad range of temperatures. It retained 25 % of its relative activity after prolonged incubation at 45°C. The specific activity of TanSg1 is enhanced by the divalent cation Ca2+ and is dramatically reduced by Zn2+ and Hg2+. The enzyme was highly specific for gallate and protocatechuate esters and showed no catalytic activity against other phenolic esters. The protein TanSg1 hydrolyzes efficiently tannic acid, a complex and polymeric gallotanin, allowing its complete conversion to gallic acid, a potent antioxidant. From its biochemical properties, TanSg1 is a tannase with potential industrial interest regarding the biodegradation of tannin waste or its bioconversion into biologically active products. © 2014 Springer-Verlag.
Versión del editorhttp://dx.doi.org/10.1007/s00253-014-5603-0
URI http://hdl.handle.net/10261/102678
DOI10.1007/s00253-014-5603-0
Identificadoresissn: 1432-0614
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