Collagen and its derivatives: From structure and properties to their applications in food industry

Tang, Cheng; Zhou, Kai; Zhu, Yichen; Zhang, Wendi; Xie, Yong; Wang, Zhaoming; Zhou, Hui; Yang, Tingting; Zhang, Qiang; Xu, Baocai

doi:10.1016/j.foodhyd.2022.107748

Cited by 89 publications

(56 citation statements)

References 219 publications

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“…The observed tissue differences and the effect of fibril formation conditions on fibrils were similar to those reported for Bester sturgeon and Amur sturgeon SC and SBC [ 1 , 5 ]. As different fibril forms may affect the hardness and other properties of biomaterials [ 16 , 41 ], the increased thickness of SC and SBC fibrils at higher NaCl concentrations and pH suggests that they may be widely applicable in biomaterial production. From the aspect of self-assembly and current results, a wider range of salinity, pH, and collagen concentration is hypothesized to help to produce more diverse fibril properties and gel materials with different characteristics.…”

Section: Resultsmentioning

confidence: 99%

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Shen

Zhang

et al. 2022

Gels

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The biochemical properties of collagens and gels from grass carp (Ctenopharyngodon idella) were studied to explore the feasibility of their application in biomaterials. The yields of skin collagen (SC) and swim bladder collagen (SBC) extracted from grass carp were 10.41 ± 0.67% and 6.11 ± 0.12% on a wet basis, respectively. Both collagens were characterized as type I collagen. Denaturation temperatures of SC and SBC were 37.41 ± 0.02 °C and 39.82 ± 0.06 °C, respectively. SC and SBC had high fibril formation ability in vitro, and higher values of salinity (NaCl, 0–280 mM) and pH (6–8) in formation solution were found to result in faster self-assembly of SC and SBC fibrils as well as thicker fibrils. Further tests of SC gels with regular morphology revealed that their texture properties and water content were affected by pH and NaCl concentration. The hardness, springiness, and cohesiveness of SC gels increased and the chewiness and water content decreased as pH increased from 7 to 8 and NaCl concentration increased from 140 to 280 mM. These properties suggest that collagens from grass carp may be useful in biomaterial applications in the future.

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Section: Resultsmentioning

confidence: 99%

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Shen

Zhang

et al. 2022

Gels

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“…A previous study of Normah and Maidzatul Afiqah [ 48 ], which reported that sin-croaker collagen represented broader band of β and γ chains in a SDS-PAGE study, also showed that the collagen had a slightly higher viscosity, compared with collagen showing narrow bands. In addition, collagen viscosity was related to the aggregation of collagen molecules resulting in the inter- or intra-protein molecular interactions [ 8 ]. The decrease in viscosity during heat-treatment may be due to a de-structure or depolymerization process of collagen molecule upon heating, the triple-helix structure within the collagen molecule that consists of hydrogen bonds in the polymer has gradually broken and transformed into the random coil configuration, resulting in the changing of physical properties [ 49 , 50 ].…”

Section: Resultsmentioning

confidence: 99%

“…Currently, approximal 28 different collagen types have been identified and characterized. They each differs greatly in amino-acid sequence, structure, and function, which are mostly a type I collagen [ 7 , 8 ]. These are distributed in different tissues, such as type-I in dermis, bones, cornea, ligaments, and tendons [ 9 ]; type-II is in the vitreous body and cartilage; type-III is in reticular fibers of lungs, vessels wall, spleen, and liver; type-IV is in basement membranes and type-V is co-distributed with type-I i.e., cornea.…”

Section: Introductionmentioning

confidence: 99%

Characteristics and Properties of Acid- and Pepsin-Solubilized Collagens from the Tail Tendon of Skipjack Tuna (Katsuwonus pelamis)

et al. 2022

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The tail tendons of skipjack tuna (Katsuwonus pelamis), a by-product from the meat-separation process in canned-tuna production, was used as an alternative source of collagen extraction. The acid-solubilized collagens using vinegar (VTC) and acetic-acid (ATC) extraction and pepsin-solubilized collagen (APTC) were extracted from tuna-tail tendon. The physiochemical properties and characteristics of those collagens were investigated. The obtained yield of VTC, ATC, and APTC were 7.88 ± 0.41, 8.67 ± 0.35, and 12.04 ± 0.07%, respectively. The determination of protein-collagen solubility, the effect of pH and NaCl on collagen solubility, Fourier-transform infrared spectroscopy (FTIR) spectrum, and microstructure of the collagen-fibril surface using a scanning electron microscope (SEM) were done. The protein solubility of VTC, ATC, and APTC were 0.44 ± 0.03, 0.52 ± 0.07, and 0.67 ± 0.12 mg protein/mg collagen. The solubility of collagen decreased with increasing of NaCl content. These three collagens were good solubility at low pH with the highest solubility at pH 5. The FTIR spectrum showed absorbance of Amide A, Amide B, Amide I, Amide II, and Amide III groups as 3286–3293 cm−1, 2853–2922 cm−1, 1634–1646 cm−1, 1543–1544 cm−1, and 1236–1237 cm−1, respectively. The SEM analysis indicated a microstructure of collagen surface as folding of fibril with small pore.

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“…A similar result was noted in [ 100 ]. This is due to the fact that these amino acid residues play a significant role in the stabilization of triple collagen-like helices [ 11 , 102 , 103 ].…”

Section: The Role Of Electrostatic Interactions Hydrogen Bonds and Hy...mentioning

confidence: 99%

Intermolecular Interactions in the Formation of Polysaccharide-Gelatin Complexes: A Spectroscopic Study

2022

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Gelatin, due to its gelling and stabilizing properties, is one of the widely used biopolymers in biotechnology, medicine, pharmaceuticals, and the food industry. One way to modify the characteristics of gelatin is molecular modification by forming non-covalent polyelectrolyte complexes with polysaccharides based on the self-organization of supramolecular structures. This review summarizes recent advances in the study of various types and the role of intermolecular interactions in the formation of polysaccharide-gelatin complexes, and conformational changes in gelatin, with the main focus on data obtained by spectroscopic methods: UV, FT-IR, and 1H NMR spectroscopy. In the discussion, the main focus is on the complexing polysaccharides of marine origin-sodium alginate, κ-carrageenan, and chitosan. The prospects for creating polysaccharide-gelatin complexes with desired physicochemical properties are outlined.

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Collagen and its derivatives: From structure and properties to their applications in food industry

Cited by 89 publications

References 219 publications

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Characteristics and Properties of Acid- and Pepsin-Solubilized Collagens from the Tail Tendon of Skipjack Tuna (Katsuwonus pelamis)

Intermolecular Interactions in the Formation of Polysaccharide-Gelatin Complexes: A Spectroscopic Study

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