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Temperature-Induced Structural Changes in Muscle Proteins from Giant Squid (Dosidicus gigas) Mantle: FT-IR, Circular Dichroism, and FE-SEM Analysis

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Publié dans:Foods vol. 14, no. 17 (2025), p. 2922-2935
Auteur principal: León-Heredia, Miguel A
Autres auteurs: Marquez-Rios, Enrique, Cadena-Cadena, Francisco, Santacruz-Ortega Hisila, Rivero-Espejel Ignacio Alfredo, Montoya-Camacho Nathaly, Tolano-Villaverde, Iván J
Publié:
MDPI AG
Sujets:
Mexico
United States > US
Japan
Dichroism
Scanning electron microscopy
Biological materials
Food
Secondary structure
Morphology
Infrared analysis
Biomaterials
Ethics
Food processing
Circular dichroism
Fourier transforms
Denaturation
Infrared spectroscopy
Proteins
Physical characteristics
Structural behavior
Nutrient content
Food industry
Giant squids
Micrography
Collagen
Spectrum analysis
Photomicrographs
Processed foods
Biomedical materials
Temperature
Electron microscopes
Field emission microscopy
Temperature effects
Protein structure
Dosidicus gigas
Accès en ligne:Citation/Abstract
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Résumé:The giant squid (Dosidicus gigas) is an abundant marine species with high protein content, making it a promising resource for the food and biomaterial industries. This study aimed to investigate the effect of temperature (25–100 °C) on the structural changes in sarcoplasmic, myofibrillar, and stromal proteins isolated from squid mantle. Fourier-transform infrared spectroscopy (FT-IR) and circular dichroism (CD) were employed to monitor modifications in secondary structure, while field emission scanning electron microscopy (FE-SEM) was used to examine morphological characteristics. The FT-IR analysis revealed temperature-induced transitions in amide I, II, and A bands, indicating unfolding and aggregation processes, particularly in myofibrillar and stromal proteins. CD results confirmed a loss of α-helix content and an increase in β-sheet structures with rising temperature, especially above 60 °C, suggesting progressive denaturation. FE-SEM micrographs illustrated clear morphological differences: sarcoplasmic proteins displayed smooth, amorphous structures; myofibrillar proteins exhibited fibrous, porous networks; and stromal proteins presented dense and layered morphologies. These findings highlight the different thermal sensitivities and structural behaviors of squid muscle proteins and provide insight into their potential functional applications in thermally processed foods and bio-based materials.
ISSN:2304-8158
DOI:10.3390/foods14172922
Source:Agriculture Science Database