Cereal Chem 40:554 - 562. | VIEW
The Mechanism of Action of Malt Beta-Glucanases. IV. The Preparation and Properties of Laminarinase from Germinated Barley.
W. W. Luchsinger, W. J.Ferrell, and G. L. Schneberger. Copyright 1963 by the American Association of Cereal Chemists, Inc.
Purified laminarinase was prepared from a 0.6% sodium chloride extract of germinated barley. The fraction which precipitated between 10 and 40% saturation in ammonium sulfate was dialyzed and the albumin: fraction was heated for 2 hr. at 50 C. The heated enzyme was further purified by chromatography on DEAE and CM-cellulose ion exchange columns. The purified laminarinase was soluble in both water and dilute salt solutions and was quite stable at 50 C. Its activity was stimulated by sodium chloride and by citrate- phosphate buffer. The enzyme exhibited a broad pH curve with an atypical sharp optimum at pH 4.59. It hydrolyzed laminarin in a random fashion, producing sugars which when chromatographed moved with glucose, laminaribiose, and gentiobiose, as well as higher oligosaccharides.