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Pilot scale preparation of wheat gluten protein fractions I‐Influence of process parameters on their protein composition
Author(s) -
BÉROT SERGE,
GAUTIER SYLVIE,
NICOLAS MICHEL,
GODON BERNARD,
POPINEAU YVES
Publication year - 1994
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1994.tb02092.x
Subject(s) - glutenin , gliadin , chemistry , gluten , chromatography , solubility , size exclusion chromatography , plant protein , acetic acid , fractionation , ultrafiltration (renal) , food science , organic chemistry , biochemistry , protein subunit , gene , enzyme
Commercial wheat gluten was fractionated on a pilot plant scale to produce gliadin‐and glutenin‐rich fractions. Acetic acid solutions (0.01–0.05 M) were blended with dry gluten (16, 10 or 7 volumes unit ‐1 of dry gluten ratio) and the slurry was separated by continuous centrifugation to yield a gliadin‐rich supernatant, which was then concentrated by ultrafiltration and spray‐dried. the pellet obtained was optionally rinsed by water or acetic acid and separated in a second stage. the second supernatant was treated as the first one, and the final residue, insoluble and glutenin‐rich, was then dispersed in ammonia and spray‐dried. the protein distributions in supernatants and residues depended on pH and ranged from 20/80 to 40/60 for the first stage, and from 40/60 to 80/20 for the sum of the two stages. the compositions of the fractions were measured by solubility tests and size exclusion high performance liquid chromatography (SE‐HPLC) profiles. A [‐1, +1] selectivity scale was created: each fraction was compared to pure gliadins (‐1), gluten (0) and pure glutenins (+1). the best combination between yields of soluble and insoluble fractions (40/60 distribution) and selectivities for gliadins and glutenins (‐0.32 and +0.26 respectively) was obtained at ratio 16 and a 0.01 M molarity. Though the selectivities were limited because gliadins and medium‐size glutenin polymers have similar solubilities in acid solutions, this process permits preparation of fractions which differ widely from gluten in contents of high molecular weight glutenin polymers.