A broad specificity beta-D-glycosidase, designated G1, was purified to homogeneity from the viscera of the China white jade snail (Achatina fulica). The enzyme was a monomeric protein with molecular weight of 115 kDa. G I has broad glycone specificity towards p-nitrophenyl derivatives Of beta-D-glucose, beta-D-fucose, beta-D-galactose, alpha-D-glucose and some disaccharides. The optimum pH and temperature are 5.5 and 55 degrees C, respectively. It was stable over a wide pH range (5-10 at 30 degrees C for 24h) and against a relatively high temperature (50 degrees C for 4h). Moreover, it was also stable and active in the presence of various alcohols. With pNPGlu, pNPFuc and cellobiose as donor, G I showed high transglycosylation activity. Six transglycosylation products were isolated from the reaction mixture containing 20% alcohol as glycoside acceptor using a preparative thin layer chromatography (preparative TLC) and identified as alkyl-glucos ides and alkyl-fucosides by mass spectrometry (MS) analysis. Combining the high alcohol tolerance, moderate temperature and pH stability and alkyl glycosides production efficiency through transglycosylation, G I can be considered to be a promising candidate for the production of various alkyl glycosides. (C) 2008 Elsevier Inc. All rights reserved.