Abstract
AbstractProteins of rye flour extracts were fractionated between pH 3 and 10 applying the electrofocusing technique both in liquid column and gel slab. The extracts for the gel study were heated to 60, 70, 90 and 100°C to study the heat inactivation of the amylolytic activity. The protein content of the fractions was determined using the UV‐absorption at 280 nm. The amylolytic activity of the column factions was studied using agar‐plate diffusion test and the activity in the gel slabs was revealed by incubation at pH 4.7 in Lintner‐starch and limit dextrin solutions, respectively, followed by iodine staining.The heat treatment was found to cause displacement of the isoelectric points of the protein fractions as detected with Coomassie‐blue staining of the gel slabs. Amylolytic activity was frequently discovered after Lintner‐starch incubation without any counterpart after that in limit dextrin. Limit dextrin treatment again independently exhibited blur zones or colour strengthening. On an α‐1,6‐glucanase activity was speculated.
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