Our obsession with high resolution in gel electrophoresis: Does it necessarily give the right answer?

Wrigley, C.W.; Gupta, Ram B.; Bekes, F.

doi:10.1002/elps.11501401191

Cited by 5 publications

(1 citation statement)

References 6 publications

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“…The multilayer SDS polyacrylamide gel electrophoresis (MLGE) method adapted from Khan and Huckle (1992) contained multilayer gels with separate zones of 4, 6, 8, 10, 12, and 14% polyacrylamide. Recipes for buffers are given in Wrigley et al (1993). Gels were stained with 0.1% (w/v) Coomassie G250 in 40% methanol and 10% acetic acid in water.…”

Section: Analysis Of Gmp Molecular Weight Distributionmentioning

confidence: 99%

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels, Molecular Weight Distribution, and Overall Composition

1999

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Cereal Chem. 76(3):395-401Changes in the amounts, molecular weight distributions, and levels of major groups of subunits in the glutenin macropolymer (GMP) of doughs during mixing were investigated. The GMP (gel protein) is the unreduced fraction of gluten protein that remains as a layer on top of the starch after extraction of SDS-soluble proteins and centrifugation. Experiments involved doughs prepared from flours derived from one weak and one strong cultivar and lines derived from cv. Olympic that were null for specific high molecular weight glutenin subunits (HMW-GS). During mixing, the amount of GMP decreased; the major changes occurred before peak mixing time (MT, achievement of peak resistance). In addition, the average apparent molecular weight of GMP (determined by both size-exclusion HPLC and multilayer gel electrophoresis) decreased during mixing, but in this case, the major changes were seen later in the mixing process, during dough breakdown. Even after extensive mixing, polymers and oligomers were released, not free glutenin subunits. During dough breakdown, the composition of GMP also changed, such that the proportion of HMW-GS decreased but β-amylases/D low molecular weight glutenin subunits (LMW-GS) increased. Changes in the total amounts of other LMW-GS typically were smaller with a decrease in the proportion of B subunits and an increase in the proportion of C subunits. The major changes in GMP composition were observed after peak MT (peak resistance) occurring earlier and to a greater extent in the weaker dough. Our results suggest that dough breakdown during mixing may be triggered by loss of HMW-GS, leading to changes in the molecular weight distribution and composition of the disulfide-bonded GMP.Covalent and noncovalent interactions between the major polypeptide constituents in dough underly the unique ability of wheat flours to form elastic, extensible dough. After initial hydration of flour through mixing with water and other components, the next step in dough development is formation of a gluten network. Glutenforming proteins deposited in protein bodies in the endosperm disrupt and become fully hydrated, forming a continuous gluten network in which starch granules are embedded. At optimal development, aggregates unfold, and a physical network of gluten polypeptides bound by both disulfide and noncovalent bonds forms (Kasarda 1989, Weegels et al 1996a. Any attempt to understand the biochemical basis for genetic and environmental differences in dough rheological behavior requires an understanding of the composition of subunit polypeptides and how they interact. Both covalent bonds (intermolecular disulfides) and noncovalent interactions are important in the formation and behavior of doughs (Ewart 1977, Ng et al 1991. However, although knowledge of the effects of variation in the allelic composition of some individual gluten polypeptides on dough quality recently has improved (reviewed by Skerritt 1998), our understanding of how polypeptides specifically interact to determine dough proper...

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Section: Analysis Of Gmp Molecular Weight Distributionmentioning

confidence: 99%

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels, Molecular Weight Distribution, and Overall Composition

1999

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Wheat Proteins

Juhász

Békés²,

Wrigley

2014

Applied Food Protein Chemistry

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Designations used by companies to distinguish their products are often claimed as trademarks. All brand names and product names used in this book are trade names, service marks, trademarks or registered trademarks of their respective owners. The publisher is not associated with any product or vendor mentioned in this book.Limit of Liability/Disclaimer of Warranty: While the publisher and author(s) have used their best efforts in preparing this book, they make no representations or warranties with respect to the accuracy or completeness of the contents of this book and specifically disclaim any implied warranties of merchantability or fitness for a particular purpose. It is sold on the understanding that the publisher is not engaged in rendering professional services and neither the publisher nor the author shall be liable for damages arising herefrom. If professional advice or other expert assistance is required, the services of a competent professional should be sought.

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Breeding cereals for quality improvement

Wrigley¹,

Morris²

1996

Cereal Grain Quality

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Our obsession with high resolution in gel electrophoresis: Does it necessarily give the right answer?

Cited by 5 publications

References 6 publications

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels, Molecular Weight Distribution, and Overall Composition

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels, Molecular Weight Distribution, and Overall Composition

Wheat Proteins

Breeding cereals for quality improvement

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