Abstract
An arbuscular endoglucanase (EC 3.2.1.4) was purified to homogeneity from roots of onion ( Allium cepa cv. Babosa) colonized by the arbuscular mycorrhizal fungus Glomus mosseae (Nicol. and Gerd.) Gerd. and Trappe. The stepwise purification procedure consisted of Filtron concentration (10 kDa), anion-exchange chromatography, anion-exchange fast protein liquid chromatography, and electroelution from polyacrylamide gels. Pure endoglucanase had a specific activity of 2500 units mg −1 protein, and was purified 198-fold with a yield of 0.6 μg enzyme g −1 root. The endoglucanase has a relative molecular weight of about 27 kDa, and behaves as a monomer in its native form.
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