Exploring the use of FTIR Amide I band deconvolution to investigate protein secondary structure and texturisation during high moisture extrusion
Fourier transform infrared spectroscopy (FTIR) combined with Amide I band deconvolution has been used to investigate protein structural changes occurring during high moisture extrusion processing (HMEP). However, it is a sensitive, user-dependent technique that has sparked debate over its appropriat...
| Autores: | , , , |
|---|---|
| Tipo de documento: | artigo |
| Data de publicação: | 2026 |
| País: | España |
| Recursos: | Institut de Recerca i Tecnologia Agroalimentàries (IRTA) |
| Repositório: | IRTA Pubpro. Open Digital Archive |
| OAI Identifier: | oai:dnet:irtapubpro__::e5380b89ff17c96e778e15eb7fc57d00 |
| Acesso em linha: | http://hdl.handle.net/20.500.12327/5087 https://doi.org/10.1016/j.saa.2026.127509 |
| Access Level: | Acceso aberto |
| Palavra-chave: | 663/664 |
| Resumo: | Fourier transform infrared spectroscopy (FTIR) combined with Amide I band deconvolution has been used to investigate protein structural changes occurring during high moisture extrusion processing (HMEP). However, it is a sensitive, user-dependent technique that has sparked debate over its appropriate analytical approach. This paper aims to assess the suitability of FTIR Amide I band deconvolution to investigate protein structural changes in fava bean protein concentrate (FBPC) caused by temperature treatment and/or HMEP at different temperatures (110 ◦C, 135 ◦C and 165 ◦C), and to explore its relationship with the texturisation level of the obtained products. Influence of sample preparation and parameter selection during FTIR deconvolution procedure was also explored. To do so, FBPC was heated in a convection oven or subjected to HMEP at different temperatures (110, 135 or 165 ◦C), and Fourier self-deconvolution (FSD) and second derivative (SD) were explored as bandnarrowing methods to analyse protein conformation from FTIR spectra. FTIR Amide I band deconvolution showed high sensitivity to sample preparation and parameter selection during FSD and SD analytical procedure. Results suggested that HMEP caused the denaturation of β-sheet forms present initially in FBPC, and an increase of other structures including intermolecular β-sheet and/or aggregates—probably due to the formation of new intermolecular bonds. Moreover, although higher temperature during HMEP enhanced fibre-like structure formation, texturisation level could not be directly related to the protein conformation of the final high moisture |
|---|