Submitted to: Meeting Abstract
Publication Type: Abstract only
Publication Acceptance Date: 6/11/2003
Publication Date: 9/28/2003
Citation: Tilley, M., Bean, S. 2003. Separation of water soluble proteins from cereals by high performance capillary electrophoresis (HPCE). Abstract No. 178 in: 2003 AACC Annual Meeting Program Book. p. 103. Meeting Abstract. Interpretive Summary: Abstract for AACC Annual Meeting to be held September 28 - October 2, 2003, in Portland, OR
Technical Abstract: Most research concerning grain proteins has concentrated upon the gluten storage proteins. The albumins and globulins are the water and salt soluble proteins that contain biologically active enzymes and enzyme inhibitors. A free zone capillary electrophoresis method was developed to separate these proteins. Optimization included sample extraction method, capillary temperature, buffer composition and additives. The optimal conditions for separation of these proteins was found to be 50 µm i.d. x 27 cm (20 cm to detector) capillary at 10 kV (with a 0.17 min ramp up time) and 25 °C. The optimum buffer was 50 mM sodium phosphate, pH 2.5 + 20% acetonitrile (v/v) (ACN) + 0.05% (w/v) hydroxypropylmethyl-cellulose (HPMC) + 50 mM hexane sulfonic acid (HSA). Sample stability was an issue that was addressed by lyophilizing fresh extracts and re-dissolving in aqueous 50% ethylene glycol and 10% separation buffer. This method was successfully used in both wheat flour and whole meal samples. Comparisons were made of several wheats of different classes as well as several cereal grains. This methodology could be useful in screening cereal grains for important enzymes and their impact on end-use quality such as food functionality, food coloration, and malting quality.