http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1692935/
Philos Trans R Soc Lond B Biol Sci. Feb 28, 2002; 357(1418): 133–142.
PMCID: PMC1692935
The structure and properties of gluten: an elastic protein from wheat grain.
This article has been cited by other articles in PMC.
Abstract
The
wheat gluten proteins correspond to the major storage proteins that are
deposited in the starchy endosperm cells of the developing grain. These
form a continuous proteinaceous matrix in the cells of the mature dry
grain and are brought together to form a continuous viscoelastic network
when flour is mixed with water to form dough. These viscoelastic
properties underpin the utilization of wheat to give bread and other
processed foods. One group of gluten proteins, the HMM subunits of
glutenin, is particularly important in conferring high levels of
elasticity (i.e. dough strength). These proteins are present in HMM
polymers that are stabilized by disulphide bonds and are considered to
form the 'elastic backbone' of gluten. However, the glutamine-rich
repetitive sequences that comprise the central parts of the HMM subunits
also form extensive arrays of interchain hydrogen bonds that may
contribute to the elastic properties via a 'loop and train' mechanism.
Genetic engineering can be used to manipulate the amount and composition
of the HMM subunits, leading to either increased dough strength or to
more drastic changes in gluten structure and properties.
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Selected References
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