A rapid spectrophotometric method for measuring insoluble glutenin content of flour and semolina for wheat quality screening

Shewry, Peter R.; Tatham, Arthur S.; Sapirstein, H. D.; Johnson, W. J.

doi:10.1039/9781847552372-00307

Cited by 5 publications

(6 citation statements)

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“…However, only one study of wheat protein was reported at near‐UV wavelength (281 nm) (Gàbor, 1989). Studies of Sapirstein and Johnson (1996, 2000) investigated usage of far‐UV wavelength at 214 nm for quantification of wheat protein groups.…”

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Rapid Assessment of Glutenin and Gliadin in Wheat by UV Spectrophotometer

et al. 2007

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Traditional breeding of common wheat (Triticum aestivum L.) concentrates largely on the improvement of protein quality because of the importance of protein in end‐product functionality, nutritional value, and economic impact. New, rapid, and inexpensive protein quality tests are required to identify premium quality families from large and diverse early‐generation breeding populations. In this study, a simple method was designed using organic solvents to divide wheat proteins into monomeric‐rich (single‐chain, mostly gliadin), polymeric‐rich (multichain, mostly low‐ and high‐molecular weight glutenin), and total soluble protein (monomeric and polymeric protein). Monomeric‐rich and total soluble protein fractions were quantified at 280 nm with an ultraviolet (UV) spectrophotometer. Protein fractions were expressed in terms of absolute concentration and as a proportion of total soluble protein. A strong linear relationship between the protein concentration in the fractions and the absorbance reading indicated that the method could accommodate a large range of protein fraction concentrations. The specific relationships between quantity and proportion of monomeric/polymeric protein fractions and dough quality tests allowed for the design of an algorithm eliminating poor quality lines from further breeding assessment. Simplicity, reliability, low cost, and a potential for automation could make this UV‐spectrophotometric method suitable for routine use in wheat breeding programs.

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confidence: 99%

Rapid Assessment of Glutenin and Gliadin in Wheat by UV Spectrophotometer

et al. 2007

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“…Two fractions of flour protein composition were determined,46 i.e., protein soluble in 50% 1‐propanol which contained mainly gliadin and insoluble glutenin which is the high molecular weight fraction of polymeric glutenin. Optimum flour water absorption (FAB), dough development time (FarDDT), farinograph stability (FarSTAB), and mixing tolerance index (MTI) were determined with a Brabender Farinograph (C.W.…”

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confidence: 99%

Models of growing season weather impacts on breadmaking quality of spring wheat from producer fields in western Canada

et al. 2008

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“…Protease activity of the sound wheat samples was determined as described by Sivri et al (1998), and was adapted from a procedure which measures the concentration of large polymeric (50PI) glutenin by UV absorbance (Sapirstein and Johnson 2000). The percentage decrease in 50PI glutenin content of a control sample of sound wheat (Canadian bread wheat cultivar Katepwa) after 1 hr of incubation with enzyme extracts of test samples was taken as the measure of the proteolytic activity.…”

Section: Protease Activitymentioning

confidence: 99%

Wheat Intercultivar Differences in Susceptibility of Glutenin Protein to Effects of Bug (Eurygaster integriceps) Protease

et al. 2002

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Cereal Chem. 79(1):41-44Preharvest bug damage to wheat can cause significant losses in breadmaking quality. One of the most prevalent forms of bug damage which frequently occurs in most countries of the Middle East, Eastern Europe and North Africa can be attributed to Heteropterous insects, particularly Eurygaster spp. Intercultivar differences in the susceptibility of glutenin to proteolytic degradation by the bug Eurygaster integriceps were investigated using six breadwheat cultivars of Turkish origin. Crude enzyme extract was prepared with distilled water from bug-damaged wheat. The freeze-dried extract was blended with sound samples of ground wheat, and the mixture was incubated in distilled water for 30 and 60 min at 37°C and subsequently freeze-dried. The proteolytic effects of bug damage were determined on large polymeric glutenin. The latter was measured as 50% 1-propanol insoluble (50PI) glutenin extractable with 50% 1-propanol in reductant dithiothreitol. The decreases in the amount of 50PI glutenin and the high and low molecular weight subunits were quantified using

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A rapid spectrophotometric method for measuring insoluble glutenin content of flour and semolina for wheat quality screening

Cited by 5 publications

References 0 publications

Rapid Assessment of Glutenin and Gliadin in Wheat by UV Spectrophotometer

Rapid Assessment of Glutenin and Gliadin in Wheat by UV Spectrophotometer

Models of growing season weather impacts on breadmaking quality of spring wheat from producer fields in western Canada

Wheat Intercultivar Differences in Susceptibility of Glutenin Protein to Effects of Bug (Eurygaster integriceps) Protease

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