种籽蛋白质的热性质.pdfVIP

Journal of Thermal Analysis and Calorimetry, Vol. 70 (2002) 833–839 THERMAL PROPERTIES OF SEED PROTEINS 1* 2 3 4 J. Magoshi , M. A. Becker , Z. Han and S. Nakamura 1 National Institute of Agrobiological Sciences and Japan Science and Technology Corporation, Tsukuba 305-8602, Japan 2Faculty of Engineering, Fukui University, Bunkyo, Fukui 910-8517, Japan 3Akita Prefecture University, Shimoshinjo, Akita 010-0146, Japan 4Faculty of Engineering, Kanagawa University, Yokohama 221-8686, Japan Abstract Thermal properties of seed proteins, prolamines from rice, wheat and soybean were studied by dif- ferential scanning calorimetry (DSC), thermogravimetry (TG), thermal expansion, X-ray diffraction and infrared spectroscopy. Prolamine films cast from aqueous ethanol are amorphous in the ran- dom-coil conformation. The glass transition of prolamine is observed at 160, 172 and 150°C for rice, wheat and soybean, respectively. The amorphous prolamine films crystallize at 196, 205 and 199°C for rice, wheat and soybean, respectively. The thermal degradation of prolamine films occurs from 228, 250 and 270°C for rice, wheat and soybean, respectively. Keywords: crystallization, DSC, glass transition, prolamine, rice, soybean, TG, thermal expansion, wheat Introduction The seeds of rice, wheat and soybean contain several kinds of proteins. These pro- teins are classified into four components according to their solubility [1]; albumin (soluble in water), globulin (soluble in saline), prolamine (soluble in alcohol) and glutelin (soluble in aqueous acid and alkali solution). Very few scientific studies have been reported on seed proteins [2], especially ones directly concerned with the struc- ture and physical properties of these proteins. We have previously studied the glass transition and crystallization of zein, the