Fractionation of the naringinase complex from Aspergillus terreus by dye affinity chromatography
2004
Soria, F. | Ellenrieder, G. | Grasselli, M. | Navarro del Canizo, A.A. | Cascone, O.
Affinity chromatography with immobilised triazine dyes was used to separate the main enzymes present in the naringinase complex produced by Aspergillus terreus CECT 2663. One α-L-rhamnosidase and two β-D-glucosidases (βG1 and βG2) were separated by a simple two-step procedure involving chromatography with Red HE-3B immobilised on Sepharose 4B first at pH 5.5 and then at pH 4.7. Maximum activity of the β-D-glucosidases was from pH 4 to 6 and at 65 °C. Both glucosidases were active on p-nitrophenol glucoside and prunin with respective Km values of 1.9 mm and 1.6 mm for βG1 and 2.1 mm and 0.25 mm for βG2. Only βG1 hydrolysed cellobiose (Km = 5.7 mm).
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