Relationship between gluten degradation by <i>Aelia</i> spp and <i>Eurygaster</i> spp and protein structure

Pérez, Gabriela; Bonet, Arturo; Rosell, Cristina M.

doi:10.1002/jsfa.2078

Cited by 28 publications

(21 citation statements)

References 24 publications

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“…Gluten is composed of proline-and glutamine-rich gliadins and glutenins that have been shown to be degraded in flour milled from Sunn pest-damaged grains (Vaccino et al, 2006). The high molecular weight glutenins have been shown by Perez et al (2005) to be more susceptible than the gliadin and low molecular weight glutenins to the insect protease. However, all are degraded.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a prolyl endoprotease from Eurygaster integriceps puton (Sunn pest) infested wheat

Darkoh

El‐Bouhssini

Baum

et al. 2010

Arch Insect Biochem Physiol

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Sunn pest, Eurygaster integriceps, Puton, infested and uninfested wheat seeds were obtained from the International Center for Agriculture Research in the Dry Areas (ICARDA), Aleppo, Syria, with the primary objective to identify the type of enzyme deposited by the Sunn pest on the wheat responsible for the gluten degradation. Enzyme levels were extremely low due to the enzyme being secreted by the insect in localized areas on the seed. Only extract from the infested wheat contained glutenase activity. Anion exchange, Cu(2+) sepharose, and gel filtration chromatography were used to partially purify and enrich protein samples from both infested wheat and uninfested wheat. An SDS-gluten assay was used to show gluten specificity while a commercially available chromogenic proline peptide, benzyloxycarbonyl-Gly-Pro-p-nitroanalide (ZGPpNA), was utilized to identify fractions containing the active proline specific enzyme activity and to determine Michaelis-Menten kinetics. Despite low levels of enzyme on the infested wheat, the enzyme was partially purified and enriched exhibiting a specific activity of 4.5 U/mg of total protein for gluten in a SDS gluten assay (1 U of enzyme activity was defined as the decrease in gel height in millimeters in 1 h) and exhibited a high-affinity Km of 65 microM for ZGPpNA, cleaving at the carboxy terminus of the proline residue. The enzyme exhibited optimal activity between pH 8 and 10.0 at temperatures between 20 degrees and 35 degrees C. The enzyme was identified to be a prolyl endoprotease.

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Section: Discussionmentioning

confidence: 99%

Characterization of a prolyl endoprotease from Eurygaster integriceps puton (Sunn pest) infested wheat

Darkoh

El‐Bouhssini

Baum

et al. 2010

Arch Insect Biochem Physiol

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“…The effect of transglutaminase addition has been also investigated for the treatment of insectdamaged flour [114]. Glutens from insect-damaged wheat were also analyzed by CZE to elucidate the mechanism of their hydrolytical degradation [115].…”

Section: Cereal Proteinsmentioning

confidence: 99%

Capillary electrophoresis of proteins 2005–2007

Dolnı́k¹

2007

Electrophoresis

152

106

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This review article with 239 references describes recent developments in capillary electrophoresis of proteins, and covers the two years since the previous review (V. Dolník, Electrophoresis 2006, 27, 126-141) through spring 2007. It includes topics related to CE of proteins, such as sample pretreatment, wall coatings, improving separation, various forms of detection, and special electrophoretic techniques including ACE, CIEF, capillary ITP, and CEC. The paper describes applications of CE to analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals and recombinant protein preparations.

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“…In bug-damaged bread wheat a marked increase of free thiol groups during initial incubation was described (Pérez et al, 2005). Results in durum wheat damaged by wheat bugs indicate that the alteration of the gliadins and glutenins initially begins with a fast depolymerisation of glutenins, independently of temperature, presumably due to a reduction of inter-chain disulphide bonds.…”

Section: Discussionmentioning

confidence: 96%

Prolamin proteins alteration in durum wheat by species of the genus Eurygaster and Aelia (Insecta, Hemiptera)

Salis

Goula

Valero³

et al. 2010

Span. j. agric. res.

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Wheat bugs are widely distributed in various areas of Europe, Asia and North Africa. Species belonging to the genus Eurygaster and Aelia pierce wheat kernels affecting protein quality. The effects of these insects' feeding activity have been studied mainly in bread wheat (Triticum aestivum L.). This study provides information on the degradation of prolamin proteins (glutenins and gliadins) of bug-damaged durum wheat (Triticum turgidum L. var durum) in six cultivars grown in Sardinia (Italy). Samples of whole flour mixture of 70% sound wheat and 30% damaged wheat were hydrated and incubated at two temperatures (45 and 4°C), for different periods of time (0, 1 and 3 h). Glutenin and gliadin content was analysed using free zone capillary electrophoresis. The presence of bug-damaged kernels had influence on the quality of durum wheat proteins. Glutenins were rapidly degraded independently to incubation temperature. Gliadin degradation, however, took place with dependence on temperature and incubation time. Therefore glutenin degradation was possibly not due solely to the activity of proteolytic enzymes but also to some other as yet unknown factor linked to wheat bugs' feeding activity.Additional key words: gliadin, glutenin, protein quality, Triticum turgidum L. var durum, wheat bugs. ResumenAlteración de las prolaminas en trigo duro por especies del género Eurygaster y Aelia (Insecta, Hemiptera)Los chinches de los cereales tienen una amplia distribución en diversas áreas de Europa, Asia y Norte de África. Especies pertenecientes a los géneros Eurygaster y Aelia se alimentan picando los granos de trigo afectando a la calidad de las proteínas. Esta alteración se ha estudiado principalmente en trigo blando (Triticum aestivum L.). El presente estudio aporta información sobre la degradación de las prolaminas (gluteninas y gliadinas) del trigo duro (Triticum turgidum L. var durum) dañado por los chinches de los cereales en seis variedades cultivadas en Cerdeña (Italia). Muestras de harina integral, con un 70% de trigo sano y un 30% de trigo dañado se incubaron a dos temperaturas (45 y 4°C), y a diferentes tiempos (0, 1 y 3 h). El contenido de las gluteninas y gliadinas se analizó mediante electroforesis capilar zonal. La presencia de granos picados por los chinches de los cereales influyó en la calidad de las proteínas del trigo duro. Las gluteninas se degradaron rápidamente, con independencia de la temperatura de incubación. En cambio, la degradación de las gliadinas resultó ser dependiente de la temperatura y del tiempo. Ante estos resultados, cabe plantearse la posibilidad de que la degradación de las gluteninas no sea debida sólo a la actividad de las proteasas sino también a algún otro factor ligado a la actividad alimenticia de los chinches de los cereales, todavía por determinar.Palabras clave adicionales: calidad de las proteínas, chinches de los cereales, gliadinas, gluteninas, Triticum turgidum L. var durum.

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Relationship between gluten degradation by Aelia spp and Eurygaster spp and protein structure

Cited by 28 publications

References 24 publications

Characterization of a prolyl endoprotease from Eurygaster integriceps puton (Sunn pest) infested wheat

Characterization of a prolyl endoprotease from Eurygaster integriceps puton (Sunn pest) infested wheat

Capillary electrophoresis of proteins 2005–2007

Prolamin proteins alteration in durum wheat by species of the genus Eurygaster and Aelia (Insecta, Hemiptera)

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