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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/55329
Title: Purification and Characterization of an Olive Fruit β-Glucosidase Involved in the Biosynthesis of Virgin Olive Oil Phenolics
Authors: Romero-Segura, Carmen ; Sanz, Carlos ; Pérez Rubio, Ana Gracia
Keywords: β-Glucosidase
Olive fruit
Virgin olive oil
Issue Date: 2009
Publisher: American Chemical Society
Citation: Journal of Agricultural and Food Chemistry 57(17): 7983-7988 (2009)
Abstract: An olive β-glucosidase was purified to apparent homogeneity from mature fruits (Olea europaea cv. Picual) by selective extraction and successive anion exchange and hydrophobic interaction chromatographic procedures. The enzyme was shown to be a homodimer made up of two identical subunits of 65.4 kDa. Optimum activity was recorded at pH 5.5 and 45 °C. The enzyme was active on the main olive phenolic glycosides, with maximum activity toward oleuropein (100%), followed by ligstroside (65%) and demethyloleuropein (21%). The enzyme showed very low activity with apigenin and luteolin glucosides and was not active on verbascoside and rutin. Kinetic values show that olive β-glucosidase is 200-fold more active against oleuropein than against the synthetic substrate p-nitrophenyl-β-d-glucopyranoside (pNPG). According to its catalytic properties, the implication of the purified olive β-glucosidase on the synthesis of virgin olive oil phenolics is discussed.
Publisher version (URL): http://dx.doi.org/10.1021/jf901293c
URI: http://hdl.handle.net/10261/55329
DOI: 10.1021/jf901293c
ISSN: 0021-8561
E-ISSN: 1520-5118
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