Cereal Chem 45:115 - 123.  |  VIEW ARTICLE
Beta-Glucosyl-Transferase from Germinated Barley.

W. W. Luchsinger and A. W. Richards. Copyright 1968 by the American Association of Cereal Chemists, Inc. 

Beta-glucosyl-transferase was prepared by chromatographing the albumin portion of 0.1N NaCl extracts of germinated barley on DEAE-cellulose. Transferase activity was exhibited when cellobiose, cellotriose, laminaribiose, laminaritriose, gentiobiose, 3-O-beta-D-cellobiosyl-D-glucose, or 3-O-beta-D-cellotriosyl-D- glucose was the substrate, but not when maltose, sucrose, or glucose was the substrate. Transferase activity was indicated by the presence on chromatograms of oligosaccharides other than the substrates. Extended incubation resulted in hydrolysis of the substrates of glucose following an initial lag phase. The hydrolysis proceeded by removal of glucose units from the nonreducing ends of the substrates. The enzyme exhibited lower Km values on trisaccharides and tetrasaccharides than on disaccharides, but higher maximum velocities on disaccharides. The highest velocity was exhibited on the beta-1,3-linked disaccharide laminaribiose.