Abstract
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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Soria, F., Ellenrieder, G., Grasselli, M. et al. Fractionation of the naringinase complex from Aspergillus terreus by dye affinity chromatography. Biotechnology Letters 26, 1265–1268 (2004). https://doi.org/10.1023/B:BILE.0000044870.99039.19
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DOI: https://doi.org/10.1023/B:BILE.0000044870.99039.19