HEAT COAGULATION OF WHEAT-FLOUR ALBUMINS AND GLOBULINS, THEIR STRUCTURE AND TEMPERATURE FRACTIONATION

Albumins and globulins were fractionated by coagulation at 70, 100, an d 120 degrees C and were studied by microscopic and electrophoretic me thods. The coagulated albumins of a U.S. commercial hard red winter (H RW) wheat blend sample included larger aggregates than those of an Isr aeli spring wheat (SW). Dialyzed globulins appeared as finger-like pat terns with embedded oil droplets and heat-coagulated globulins appeare d as aggregates with fibril-like patterns. An increase in size of coag ulated aggregates was observed as temperatures increased (70, 100, and 120 degrees C). Differences in capillary zone electrophoresis (CZE) a nd sodium dodecyl sulfate (SDS)- polyacrylamide gel electrophoresis (P AGE) patterns between coagulates from samples of an Israeli SW and a U .S. commercial HRW wheat were seen at all the coagulation temperatures . SDS-PAGE patterns of coagulates obtained at lower temperatures exhib ited relatively more intense bands of higher molecular weight componen ts, and those obtained at higher temperatures exhibited relatively mor e intense bands of lower molecular weights. (C) 1995 Academic Press Li mited