PURIFICATION OF AN ARBUSCULAR MYCORRHIZAL ENDOGLUCANASE FROM ONION ROOTS COLONIZED BY GLOMUS-MOSSEAE

An arbuscular endoglucanase (EC 3.2.1.4) was purified to homogeneity f rom roots of onion (Allium cepa cv. Babosa) colonized by the arbuscula r mycorrhizal fungus Glomus mosseae (Nicol. and Gerd.) Gerd. and Trapp e. The stepwise purification procedure consisted of Filtron concentrat ion (10 kDa), anion-exchange chromatography, anion-exchange fast prote in liquid chromatography, and electroelution from polyacrylamide gels. Pure endoglucanase had a specific activity of 2500 units mg(-1) prote in, and was purified 198-fold with a yield of 0.6 mu g enzyme g(-1) ro ot. The endoglucanase has a relative molecular weight of about 27 kDa, and behaves as a monomer in its native form. Copyright (C) 1996 Elsev ier Science Ltd