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Collagen, the most abundant and widely distributed functional protein in mammals, typically assembles into collagen fibrils through side-by-side packing. The purpose of this study was to comparatively investigate the fate of sea cucumber collagen fibrils in the gastrointestinal tract when interacting with different anionic polysaccharides (fucoidan (FUC), Kappa-carrageenan (K-car), sodium alginate (SA)). Results revealed that the gel properties and viscosity values of collagen fibrils were notably enhanced, and the rate of structural alteration in collagen fibrils was reduced when K-car and SA were introduced. Conversely, in the presence of FUC, collagen fibril viscosity decreased, and the secondary structure of collagen fibrils underwent changes. FUC was found to diminish the structural stability of collagen fibrils and accelerate the gastric digestion rate, which was further exacerbated by thermal treatment. All these anionic polysaccharides were observed to facilitate the formation of collagen peptide aggregates by binding to polysaccharides during intestinal digestion. This study bridged the knowledge gap regarding the impact of anionic polysaccharides on the gastrointestinal digestion of collagen fibrils, potentially paving the way for broader applications of collagen in the food industry. • The structure and digestion fate of sea cucumber collagens was investigated. • The presence of anionic polysaccharides inconsistently regulated collagen fibrils. • The presence of fucoidan (FUC) improved gastrointestinal digestion rate of fibrils. • Heat treatment increased the effect of FUC on digestion rate of collagen fibrils. • The presence of Kappa-carrageenan and sodium alginate reduced the digestion rate. [ABSTRACT FROM AUTHOR]

Collagen, the most abundant and widely distributed functional protein in mammals, typically assembles into collagen fibrils through side-by-side packing. The purpose of this study was to comparatively investigate the fate of sea cucumber collagen fibrils in the gastrointestinal tract when interacting with different anionic polysaccharides (fucoidan (FUC), Kappa-carrageenan (K-car), sodium alginate (SA)). Results revealed that the gel properties and viscosity values of collagen fibrils were notably enhanced, and the rate of structural alteration in collagen fibrils was reduced when K-car and SA were introduced. Conversely, in the presence of FUC, collagen fibril viscosity decreased, and the secondary structure of collagen fibrils underwent changes. FUC was found to diminish the structural stability of collagen fibrils and accelerate the gastric digestion rate, which was further exacerbated by thermal treatment. All these anionic polysaccharides were observed to facilitate the formation of collagen peptide aggregates by binding to polysaccharides during intestinal digestion. This study bridged the knowledge gap regarding the impact of anionic polysaccharides on the gastrointestinal digestion of collagen fibrils, potentially paving the way for broader applications of collagen in the food industry. • The structure and digestion fate of sea cucumber collagens was investigated. • The presence of anionic polysaccharides inconsistently regulated collagen fibrils. • The presence of fucoidan (FUC) improved gastrointestinal digestion rate of fibrils. • Heat treatment increased the effect of FUC on digestion rate of collagen fibrils. • The presence of Kappa-carrageenan and sodium alginate reduced the digestion rate. [ABSTRACT FROM AUTHOR]

Gel properties of hydrogel-forming by Ala-Lys dipeptide (AK) and iota-carrageenan (ι-C) were investigated by rheological behavior, fourier transform infrared analysis, cryo-scanning electron microscopy, low field-NMR relaxometry and magnetic resonance imaging. Iota-carrageenan was changed from a liquid to a gel with the addition of AK, and the existence of AK significantly increased the storage modulus (G') of ι-C from 590.4 to 1077.8 Pa. In the ι-C/AK gel, the blue-shift of O H stretching and water deformation were observed, meanwhile, the presence of amide I band at 1682 cm−1 was observed. The network of ι-C/AK gel showed a dense honeycomb structure with flocculating continuous phase and rough entanglement morphology. After adding AK, the water free in the pores of ι-C entered the ι-C/AK gel matrix, and the binding capacity of bound water was enhanced. These scenarios proved that the AK as the cationic dipeptide could control the conversion of negatively charged ι-C from an original random structure to a helical structure due to electrostatic interactions and hydrogen bonds. This study provides a new opportunity for the peptides into carbohydrate-based gel matrices, which could provide insights for the further application of ι-C/AK gels in the fields of food industry, tissue engineering and drug delivery. • AK dipeptide enhanced the gel properties of iota-carrageenan. • Electrostatic interactions was the main force in AK/ ι-C gel. • The hydrogen bond stabilized the AK/ι-C gel structure. • AK induced regular and homogenous network structure in the ι-C gel. [ABSTRACT FROM AUTHOR]