Collagen as a source of bioactive peptides: A bioinformatics approach

Nuñez, Suleivys M.; Guzmán, Fanny; Valencia, Pedro; Almonacid, Sergio; Cárdenas, Constanza

doi:10.1016/j.ejbt.2020.09.009

Cited by 27 publications

(24 citation statements)

References 45 publications

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“…Collagen has a triple helix structure stabilized by hydrogen bonds and covalent crosslinkages with other collagen molecules, which limits its applications considerably [9] . The key to obtaining antioxidant peptides is to break the triple helix structure of collagen and ensure the maximum release of active peptides during hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Gao

Wang

et al. 2021

Ultrasonics Sonochemistry

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Section: Introductionmentioning

confidence: 99%

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Gao

Wang

et al. 2021

Ultrasonics Sonochemistry

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“…The production process transforms collagen into water-soluble gelatin [ 98 ]. Collagen determines the physicochemical properties of gelatin, and in particular, the gel strength of the obtained proteins [ 99 ]. Collagen is a protein with an unusual amino acid composition.…”

Section: The Most Common Sources Of Plant and Animal Proteinsmentioning

confidence: 99%

Proteins in Food Systems—Bionanomaterials, Conventional and Unconventional Sources, Functional Properties, and Development Opportunities

2021

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Recently, food companies from various European countries have observed increased interest in high-protein food and other products with specific functional properties. This review article intends to present proteins as an increasingly popular ingredient in various food products that frequently draw contemporary consumers’ attention. The study describes the role of conventional, unconventional, and alternative sources of protein in the human body. Furthermore, the study explores proteins’ nutritional value and functional properties, their use in the food industry, and the application of proteins in bionanomaterials. Due to the expected increase in demand for high-protein products, the paper also examines the health benefits and risks of consuming these products, current market trends, and consumer preferences.

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“…According to M. Gauza-Włodarczyk [ 40 ], certain differences were also established between fish collagen and cattle collagen when comparing their thermal properties. It is notable that analysis, using a bioinformatic analysis, of collagen from five sources of various origins revealed their differences, these being most pronounced between phylogenetically distant species, for example, between pigs and fish [ 41 ]. That is, the nature of the substrate from which the biopolymer is isolated largely determines its properties.…”

Section: Introductionmentioning

confidence: 99%

Changes in the Molecular Characteristics of Bovine and Marine Collagen in the Presence of Proteolytic Enzymes as a Stage Used in Scaffold Formation

et al. 2021

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Biopolymers, in particular collagen and fibrinogen, are the leading materials for use in tissue engineering. When developing technology for scaffold formation, it is important to understand the properties of the source materials as well as the mechanisms that determine the formation of the scaffold structures. Both factors influence the properties of scaffolds to a great extent. Our present work aimed to identify the features of the molecular characteristics of collagens of different species origin and the changes they undergo during the enzymatic hydrolysis used for the process of scaffold formation. For this study, we used the methods of gel-penetrating chromatography, dynamic light scattering, reading IR spectra, and scanning electron microscopy. It was found that cod collagen (CC) and bovine collagen (BC) have different initial molecular weight parameters, and that, during hydrolysis, the majority of either type of protein is hydrolyzed by the proteolytic enzymes within the first minute. The differently sourced collagen samples were also hydrolyzed with the formation of two low molecular fractions: Mw ~ 10 kDa and ~20 kDa. In the case of CC, the microstructure of the final scaffolds contained denser, closely spaced fibrillar areas, while the BC-sourced scaffolds had narrow, short fibrils composed of unbound fibers of hydrolyzed collagen in their structure.

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Collagen as a source of bioactive peptides: A bioinformatics approach

Cited by 27 publications

References 45 publications

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Proteins in Food Systems—Bionanomaterials, Conventional and Unconventional Sources, Functional Properties, and Development Opportunities

Changes in the Molecular Characteristics of Bovine and Marine Collagen in the Presence of Proteolytic Enzymes as a Stage Used in Scaffold Formation

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