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               <dc:title>Exploring the use of FTIR Amide I band deconvolution to investigate protein secondary structure and texturisation during high moisture extrusion</dc:title>
               <dc:creator>Barnés Calle, Clara</dc:creator>
               <dc:creator>Gou, Pere</dc:creator>
               <dc:creator>Fulladosa, Elena</dc:creator>
               <dc:creator>van den Berg, Frans W.J.</dc:creator>
               <dc:contributor>Indústries Alimentàries</dc:contributor>
               <dc:contributor>Qualitat i Tecnologia Alimentària</dc:contributor>
               <dc:description>Fourier transform infrared spectroscopy (FTIR) combined with Amide I band deconvolution has been used to&#xd;
investigate protein structural changes occurring during high moisture extrusion processing (HMEP). However, it&#xd;
is a sensitive, user-dependent technique that has sparked debate over its appropriate analytical approach. This&#xd;
paper aims to assess the suitability of FTIR Amide I band deconvolution to investigate protein structural changes&#xd;
in fava bean protein concentrate (FBPC) caused by temperature treatment and/or HMEP at different temperatures&#xd;
(110 ◦C, 135 ◦C and 165 ◦C), and to explore its relationship with the texturisation level of the obtained&#xd;
products. Influence of sample preparation and parameter selection during FTIR deconvolution procedure was&#xd;
also explored. To do so, FBPC was heated in a convection oven or subjected to HMEP at different temperatures&#xd;
(110, 135 or 165 ◦C), and Fourier self-deconvolution (FSD) and second derivative (SD) were explored as bandnarrowing&#xd;
methods to analyse protein conformation from FTIR spectra. FTIR Amide I band deconvolution&#xd;
showed high sensitivity to sample preparation and parameter selection during FSD and SD analytical procedure.&#xd;
Results suggested that HMEP caused the denaturation of β-sheet forms present initially in FBPC, and an increase&#xd;
of other structures including intermolecular β-sheet and/or aggregates—probably due to the formation of new&#xd;
intermolecular bonds. Moreover, although higher temperature during HMEP enhanced fibre-like structure formation,&#xd;
texturisation level could not be directly related to the protein conformation of the final high moisture</dc:description>
               <dc:date>2026-02-28T23:30:50Z</dc:date>
               <dc:date>2026-02-28T23:30:50Z</dc:date>
               <dc:date>2026-01-21</dc:date>
               <dc:type>info:eu-repo/semantics/article</dc:type>
               <dc:identifier>1386-1425</dc:identifier>
               <dc:identifier>https://hdl.handle.net/20.500.12327/5087</dc:identifier>
               <dc:identifier>https://doi.org/10.1016/j.saa.2026.127509</dc:identifier>
               <dc:language>eng</dc:language>
               <dc:relation>Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy</dc:relation>
               <dc:relation>MICINN/Programa Estatal para impulsar la investigación científico-técnica y su transferencia/PID2021-122285OR-I00/ES/Sensors and algorithms to optimize high moisture meat analogue production when using novel protein sources/SENSANALOG</dc:relation>
               <dc:relation>EC/H2020/101000847/EU/Climate Resilient Orphan croPs for increased DIVersity in Agriculture/CROPDIVA</dc:relation>
               <dc:relation>FEDER/ / /EU/ /</dc:relation>
               <dc:relation>ESF/ / /EU/ /</dc:relation>
               <dc:relation>EC/COST/CA19145/EU/European Network for assuring food integrity using non-destructive spectral sensors/SensorFINT</dc:relation>
               <dc:rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</dc:rights>
               <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
               <dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights>
               <dc:publisher>Elsevier</dc:publisher>
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