The varietal differences in some biological activities of proteins extracted from flours of wheat seeds harvested in 1986.
Six wheat seeds varieties taken for experiments showed some differences in crude protein content ranging from 10.4-12.8%. A procedure for protein fractionation by the successive elimination of albumins, globulins and gliadins from the wheat varieties studied was elaborated. In the obtained protein fractions endogenous amylolytic and inhibitory activities tested against bovine pancreas trypsin and alpha-amylases of mammalian and insect origin were determined. The determined biological activities differ considerable among wheat varieties studied and were mainly located in albumins and gliadins while only a small amount were detected in globulins. Extractable proteins were relatively thermostabile and powerful inhibitors of the alpha-amylases examined. As the influence of environmental conditions was the same for all wheat varieties studied the observed differences in biological activities should be rather attributed to the genetic differences.
Warchalewski
J R
JR
University of Agriculture, Faculty of Food Technology, Institute of Microbiology, Biochemistry and Food Analysis, Poznań, Poland.
Madaj
D
D
Skupin
J
J
D000418:Albumins / Q000302:isolation & purification; D000818:Animals; D005591:Chemical Fractionation; D005433:Flour / Q000032:analysis*; D005903:Gliadin / Q000302:isolation & purification; D005916:Globulins / Q000302:isolation & purification; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D012639:Seeds / Q000032:analysis*; D014908:Triticum / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000494:pharmacology; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000378:metabolism; D001614:beta-Amylase / Q000378:metabolism
D000418:Albumins; D005916:Globulins; D010940:Plant Proteins; D014361:Trypsin Inhibitors; D005903:Gliadin; D000516:alpha-Amylases; D001614:beta-Amylase