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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Xuất bản năm:	Foods vol. 14, no. 17 (2025), p. 2922-2935
Tác giả chính:	León-Heredia, Miguel A
Tác giả khác:	Marquez-Rios, Enrique, Cadena-Cadena, Francisco, Santacruz-Ortega Hisila, Rivero-Espejel Ignacio Alfredo, Montoya-Camacho Nathaly, Tolano-Villaverde, Iván J
Được phát hành:	MDPI AG
Những chủ đề:	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
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Miêu tả
Bài tóm tắt:	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.
số ISSN:	2304-8158
DOI:	10.3390/foods14172922
Nguồn:	Agriculture Science Database