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ABSTRACT
A modified procedure for the extraction of α-zein from corn gluten meal was developed and compared against a commercial extraction method. The modification involved raising the concentration of alcohol in solvent and removing the precipitate by centrifugation. Five organic solvent mixtures were compared using the modified extraction procedure developed along with the reductant sodium bisulfite and NaOH. The modified procedure precipitated most of the non-a-zein protein solids by increasing the concentration of alcohol. The supernatant had a-zein-rich fraction, resulting in higher yield of a-zein than the commercial method when cold precipitated. The commercial extraction procedure had a zein yield of 23% and protein purity of 28% using 88% 2-propanol solvent. The three best solvents, 70% 2-propanol, 55% 2-propanol, and 70% ethanol, yielded =35% of zein at protein purity of 44% using the modified extraction procedure. Zeins extracted using the novel method were lighter in color than the commercial method. Densitometry scans of SDS-PAGE of a-zein-rich solids showed relatively large quantities of a-zein with apparent molecular weights of 19,000 and 22,000 Da. The a-zein-rich solids also had small amounts of d-zein (10,000 Da) because it shares similar solubility properties to a-zein. A solvent mixture with 70% 2propanol, 22.5% glycerol, and 7.5% water extracted significantly less zein (-33%) compared to all other solvents and had a-zein bands that differed in appearance and contained little to no δ-zein.
Cereal Chem. 88(4):356-362
Zein is <52% protein by weight in the corn kernel. Zein proteins were first described by Gorham (1821), who extracted them from Indian com. Interest in the protein developed when Osbome (1891) extracted zein from com gluten meal (CGM), which was a high-protein coproduct of corn wet milling. Later, Osborne and Mendel (1914) classified protein from com into four different categories based on solubility. These proteins were albumins (soluble in pure water), globulins (soluble in aqueous salt solutions), prolamins (soluble in 70% ethanol), and glutelins (soluble in dilute acid or base). Zein proteins are prolamins and have been further characterized into four different classes based on solubility, electrophoresis, and immunological studies. Esen (1987, 1990) classified them as a, β, γ, and d-zein. Important past applications of zein were in inks, adhesives, coatings, plastics, and chewing gums (Sturken 1938; Coleman 1939, 1941; Lougovoy 1949; Simonds...