Isolation and functionality testing of low molecular weight glutenin subunits

• Published in: Cereal chemistry Vol. 75; no. 1
• Main Authors: Sissons, M.J. (CSIRO Division of Plant Industry, Canberra, ACT, Australia.), Bekes, F, Skerritt, J.H
• Format: Journal Article
• Language: English
• Published: 01.01.1998
• Subjects: AMINO ACID SEQUENCES; APTITUDE BOULANGERE; BAKING CHARACTERISTICS; BREADMAKING; CARACTERISTICAS DE LA COCCION; CHEMICAL COMPOSITION; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; DOUGHS; FARINE DE BLE; GLUTENINAS; GLUTENINE; GLUTENINS; GRAIN; GRANOS; HARINA DE TRIGO; MASA DE PANADERIA; MELANGE; MEZCLADO; MIXING; MOLECULAR WEIGHT; PANIFICACION; PANIFICATION; PATE DE CUISSON; PESO MOLECULAR; POIDS MOLECULAIRE; PURIFICACION; PURIFICATION; WHEAT FLOUR; WHOLE GRAINS
• ISSN: 0009-0352; 1943-3638
• DOI: 10.1094/CCHEM.1998.75.1.30

Various protein fractionation techniques have been applied to the isolation and purification of milligram quantities of low molecular weight glutenin subunits ( LMW-GS). No single technique was applicable to the purification of the majority of the subunits. Partial purification of certain LMW-GS was obtained using ion-exchange chromatography and reversed-phase HPLC. Preparations containing alpha- and gamma-type subunit sequences did not strengthen dough when incorporated into a base flour, whereas preparations containing a subunit with an N-terminal methionine residue (METSHIPGL-) did. Using preparative isoelectric focusing over a narrow pH range, it was possible to purify (to approximately 90% purity) a B subunit that also had the N-terminal sequence of METSHIPGL-. This polypeptide, when incorporated into a base flour, had a dough strengthening effect in mixing trials, but less so than an equivalent amount of a high molecular weight glutenin subunit