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Impact of extrusion-induced protein molecular rearrangement on cooking qualities, in vitro digestibility and gluten allergenicity of durum wheat pasta
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The cooking quality and digestibility of pasta are influenced by its protein structures. However, how shear forces affect protein molecular structure leading to pasta quality and the allergenicity of pasta is not well understood. This study explored the impact of varying screw speeds (150 rpm and 550 rpm), which directly influence specific mechanical energy (SME) input during extrusion, on protein molecular weight distribution, cooking properties, and starch and protein digestibility in both regular durum wheat pasta and gluten-enriched pasta. Pasta produced at 550 rpm exhibited reduced water absorption and cooking time but significantly increased cooking loss, accompanied by a decrease in disulphide bonds. Size-exclusion chromatography (SEC) and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) results indicated that high screw speed caused the insolubility of glutenins and globulins while increasing the solubility of gliadins. Additionally, these structural changes corresponded to decreased ionic and hydrogen bonding and increased hydrophobic interactions. Although starch and protein enzymic digestibility was decreased with added gluten, the increased screw speed enhanced their digestion. Proteomic mapping by liquid chromatography-tandem mass spectrometry (LC-MS/MS analysis) revealed a reduction in the number of identified proteins and allergens in the digestate of pasta produced at 550 rpm, while the number of identified peptides increased. Additionally…
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This suggests a softening phase that may facilitate processing operations requiring improved material flow, such as mixing, moulding, extrusion.
“Notably, FB-90-US exhibited an initial reduction in G ′ and G ″ , suggesting a softening phase that may facilitate processing operations requiring improved material flow, such as mixing, moulding, extrusion (Devkota et al., 2025; Jia et al., 2025; Rodrigues et al., 2026; Shrestha et al., 2024).”
From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Jia et al., 2025
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Zhu, M., Kasapis, S., & Dhital, S. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113251
Self-citation
Metadata
- Authors
- Jia, B., Devkota, L., Sissons, M., Attenborough, E., Ni, D., & Dhital, S.
- Affiliations
- Monash University (AU)
- New South Wales Department of Primary Industries (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Corresponding author
- Dhital, Sushil
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2025-11
- Volume
- 492
- Issue
- Pt 1
- Pages
- 145293
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W4411589441
- Cited by
- 7
- References
- 0
- Citations by year
- 2026: 6 · 2025: 1
- FWCI
- 3.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Food Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Monash University
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Health Sciences › Medicine › Gastroenterology › Celiac Disease Research and Management
- Keywords
- durum wheat pasta, extrusion, screw speed, protein structure, gluten, cooking quality, in vitro digestibility, starch digestibility, disulfide bonds, glutenin, gliadin, globulin, hydrophobic interactions, gastric digestion, proteolysis, specific mechanical energy
- MeSH terms
- Allergens, Cooking, Digestion, Flour, Glutens, Hot Temperature, Humans, Plant Proteins, Triticum
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