Thermally induced gluten modification observed with rheology and spectroscopies

Wehrli, Monika C.; Kratky, Tim; Schopf, Marina; Scherf, Katharina Anne; Becker, Thomas; Jekle, Mario

doi:10.1016/j.ijbiomac.2021.01.008

Cited by 20 publications

(12 citation statements)

References 49 publications

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“…Importantly, during water vapor annealing, the 3D structures of scaffold was stabilized due to crystallization by induction of hydrogen bonding between macromolecules. As is the case in many recent findings, water is used as plasticizer to establish hydrogen bonds in the protein system. ,, Adding hydrogen bonds increases the number of β-sheets in the protein’s crystalline region, which helps the protein create a stable 3D structure. ,, The FTIR results demonstrated that the fibril scaffolds had less random coil content and more β-sheet formation following water annealing (Figure D), which suggested the role of intramolecular hydrogen bonding . As the water molecules are eliminated (drying), it also causes the protein molecules that are scattered in the aqueous solution to become more spatially compact .…”

Section: Discussionmentioning

confidence: 69%

“…30,64,65 Adding hydrogen bonds increases the number of β-sheets in the protein's crystalline region, which helps the protein create a stable 3D structure. 30,66,67 The FTIR results demonstrated that the fibril scaffolds had less random coil content and more β-sheet formation following water annealing (Figure 3D), which suggested the role of intramolecular hydrogen bonding. 44 As the water molecules are eliminated (drying), it also causes the protein molecules that are scattered in the aqueous solution to become more spatially compact.…”

Section: Discussionmentioning

confidence: 99%

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Soy Protein Amyloid Fibril Scaffold for Cultivated Meat Application

Wei

Dai

Huang

et al. 2023

ACS Appl. Mater. Interfaces

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It is important to have sustainable and edible scaffolds to produce cultivated meat. In this research, three-dimensional (3D) porous scaffolds were developed by soy protein amyloid fibrils for cultivated meat applications. Food-safe biological and physical cross-linking methods using microbial transglutaminase and temperature-controlled water vapor annealing technique were employed to crosslink soy protein amyloid fibrils, resulting in the production of 3D scaffolds. The generated 3D scaffolds had pores with sizes ranging from 50 to 250 μm, porosities of 72–83%, and compressive moduli of 3.8–4.2 kPa, depending on the type of soy protein used in the process (β-conglycinin (7S), glycinin (11S) and soy protein isolate (SPI)). When present with pepsin, these scaffolds can degrade within an hour but remain stable in phosphate-buffered saline for at least 30 days. The soy protein amyloid fibril scaffolds enabled C2C12 mouse skeletal myoblasts proliferate and differentiate without adding cell adhesive proteins or other coatings. The results demonstrate the potential of abundant and inexpensive soy protein amyloid fibrils to be utilized as scaffold materials for cultivated meat in the food industry.

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Section: Discussionmentioning

confidence: 69%

Section: Discussionmentioning

confidence: 99%

Soy Protein Amyloid Fibril Scaffold for Cultivated Meat Application

Wei

Dai

Huang

et al. 2023

ACS Appl. Mater. Interfaces

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“…Fessas and Schiraldi [ 44 ] have shown that the bound water fraction, which mainly interacts with gluten, was released with a maximum rate reached at 125 °C. Wehrli et al [ 45 ] also found that water tightly linked to gluten was removed at temperatures between 100 and 300 °C and highlighted that, around 250 °C, phenomena of pyrolysis of the matrix material occur, with the release of CO 2 groups and volatile hydrocarbon species due to the decarboxylation and degradation of proteins. Therefore, the second important weight loss recorded in the TGA curves was due to the thermal decomposition of the dough, which proceeds up to 400 °C and beyond [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

Study of Physico-Chemical Properties of Dough and Wood Oven-Baked Pizza Base: The Effect of Leavening Time

Covino

Sorrentino

Pierro

et al. 2023

Foods

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The research objective was to investigate the morpho-rheological, chemical, and structural changes of dough and Neapolitan pizza TSG as the leavening time varies and to evaluate their effects on the digestibility of starch and on the formation of acrylamide during baking. Pizza dough leavening was monitored for 48 h at 22 °C/80% RH, and the analyses were conducted at selected leavening times (0, 4, 8, 16, 24, and 48 h). It was observed that in 30 h the volume tripled and the viscoelastic dough relaxed in the first 4 h, as evidenced by the lower value of the relaxation percentage “a” and the higher rate of decay “b”, associated with a high value of the compression work, indicating the presence of a very strong gluten mesh. In the following hours, the dough lost elasticity, and in fact, the G’ modulus decreased due to the weakening of the weak interactions between the gluten proteins and the starch. This suggests that a long leavening improved the extensibility of the pizza disc, facilitating the action of the pizza maker. Thermal (TGA and DSC) and morphological (SEM) analyses evidenced the highest water removal rate from the dough, a wider starch gelatinization temperature range, a ∆H of 0.975 ± 0.013 J/g, and a more open and weak gluten structure in dough balls leavened for 16 h. As the leavening time increased, both dough and pizza base samples showed an increase in reducing sugars and free amino groups, while the rapidly digestible starch decreased in the dough following the metabolism of the yeasts and increased in the pizza base due to the starch gelatinization that occurs during baking, which makes it much more susceptible to α-amylase. Finally, the levels of acrylamide remained at the same values despite the higher availability of reducing sugars and its precursors during leavening.

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“…Surface chemical composition of WG and PP-WG samples were characterized by the ESCALAB250Xi X-ray photoelectron spectrometer (XPS) (Thermo Fisher, USA) equipped with Al K-alpha radiation X-rays of 300 W and monochromatic Kα source (hν = 1486.6 eV, 250 W) basing on the approach as described by Wehrli et al (2021) . The spectrum of each element was determined with a resolution of 0.05 eV and pass energy was 25 eV.…”

Section: Methodsmentioning

confidence: 99%