2018
DOI: 10.1016/j.foodhyd.2018.07.020
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Characteristics of the chemical processes induced by celluloses in the model and gluten dough studied with application of FTIR spectroscopy

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Cited by 35 publications
(18 citation statements)
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“…In order to determine the structural changes in the powders studied, difference spectra in the spectral regions of 900-1 800 and 2 400-3 800 cm -1 were calculated according to Nawrocka et al (2018). Briefly, all spectra were band area-normalized, and then the spectrum of the control sample was subtracted from the spectra of the moisturized samples.…”
Section: Methodsmentioning
confidence: 99%
“…In order to determine the structural changes in the powders studied, difference spectra in the spectral regions of 900-1 800 and 2 400-3 800 cm -1 were calculated according to Nawrocka et al (2018). Briefly, all spectra were band area-normalized, and then the spectrum of the control sample was subtracted from the spectra of the moisturized samples.…”
Section: Methodsmentioning
confidence: 99%
“…Additionally, analysis of the β-sheets region in the amide III band can provide information about two types of hydrogen bonds (type I and type II) [ 32 ] formed during dough mixing. According to Nawrocka et al [ 33 ], the type I hydrogen bonds (–HN···O=C–) with a band at ca. 1230 cm −1 can be formed between polypeptide chains in the gluten network leading to its aggregation, whereas H bonds of type II (–HN···O, ether bond) with a band at ca.…”
Section: Spectroscopic Methods Used In the Study Of Gluten Structumentioning
confidence: 99%
“…Cellulose and inulin as water insoluble polysaccharides led to formation of pseudo-β-sheets, whereas water soluble pectins induced formation of hydrated/extended β-sheets. Differences in the gluten structure between gluten dough and model dough were observed by Nawrocka et al [ 33 ] as a result of supplementation of both doughs with celluloses differing in particle size and chemical structure. Analysis of the FT-IR spectra of the control gluten dough showed presence of the bands assigned to hydrated β-sheets and water microvoids which indicate proper hydration level of the gluten network.…”
Section: Factors Affecting Structure Of Gluten Network Gliadins Amentioning
confidence: 99%
“…However, high-molecular-weight glutenin subunits participating in the depolymerization reaction facilitate a weakened gluten network, resulting in decreased resistance to extension. Additionally, gluten secondary structure plays an important role in the gluten network (Nawrocka et al, 2018;Wang et al, 2018) and affects the extensographic properties of dough. Wellner et al (2005) revealed that glutenins primarily contributed to β-structures (β-sheets and β-turns), while gliadins primarily contributed to the α-helix structure.…”
Section: Extensograph Properties Of Steamed Bread Doughmentioning
confidence: 99%