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Utilization of Fisheries' By-Products for Functional Foods
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Muhamad Darmawan, Nurrahmi Dewi Fajarningsih, Sihono, Hari Eko Irianto
Gelatin is a fibrous protein derived from hydrolytic degradation of collagen, which is obtained from cartilages, skin, bones and connective tissues of various animals (Akbar et al., 2017). As a functional biopolymer, gelatin has very extensive applications in industries ranging from pharmaceuticals, cosmetics, materials, foods and photography depend on their rheological properties, that is, transparency, solubility, viscosity, gel strength and thermal stability. Moreover, the application of gelatin as functional foods is also expanding (Karim and Bhat, 2009; Gomez-Guillen et al., 2011). The global demand of gelatin is constantly increasing. World gelatin production reached 450,000 tons in 2018 with an estimated value of US$4.52 billion (Tkaczewska et al., 2018).
Microplastic and Nanoplastic Pollution in Water Bodies from Conventional Packaging Materials
Published in Arbind Prasad, Ashwani Kumar, Kishor Kumar, Biodegradable Composites for Packaging Applications, 2023
Gelatin is a protein-based polymer that is derived from collagen of pigs and cows. It has a random coil conformation at elevated temperatures, whereas at lower temperatures, it forms helix. Its sensitiveness to temperature allows it to form viscous sols and thermo-reversible gels when heated and cooled, respectively. The incorporation of gelatin improves the barrier properties, transparency and mechanical properties of starch-based films and other biocomposite films [1,29].
Polysaccharides and Proteins-based Hydrogels for Tissue Engineering Applications
Published in Rajesh K. Kesharwani, Raj K. Keservani, Anil K. Sharma, Tissue Engineering, 2022
Roberta Cassano, Federica Curcio, Maria Luisa Di Gioia, Debora Procopio, Sonia Trombino
Gelatin (Figure 8.7) is a protein-based material derived from the hydrolysis of collagen. It is very useful in biomedical and pharmaceutical fields (Jain and Kumar, 2013; Tonsomboon et al., 2013) due to its biodegradable, biocompatible nature, low immunogenicity, and its commercial availability at low cost. The advantages include its solubility in aqueous systems, a sol–gel transition at 30 °C (Bohidar and Jena, 1994), and the possibilty to be cross-linked or modified with the inclusion of other materials to significantly alter its mechanical and biochemical properties (Jain and Kumar, 2013).
Regenerated silk fibroin loaded with natural additives: a sustainable approach towards health care
Published in Journal of Biomaterials Science, Polymer Edition, 2023
Niranjana Jaya Prakash, Xungai Wang, Balasubramanian Kandasubramanian
Gelatin belongs to the class of natural proteins and is isolated from collagen present in animal tissues. Even though they are produced from animal tissues, they generally don’t show any immunogenic responses since the hydrolysis process offers them a very low antigenicity. Gelatin is found to be highly biocompatible, biodegradable, and on degradation, they generate non-toxic metabolic products. However, the use of gelatin presents a potential risk of transmitting infectious diseases; in order to rectify this, genetically modified human recombinant gelatin has come into the picture [58]. Gelatin can be successfully incorporated into silk fibroin for the formation of hydrogels, tubes, and films. SF/gelatin hydrogels can be easily synthesized in an aqueous solution with the introduction of methanol. Tubes of gelatin hydrogels were also synthesized, which displayed mechanical properties similar to that of arteries on reinforcing with silk fibroin. Further studies have also shown the possibility of preparing microporous films of silk fibroin with the dissolution of gelatin in a saline solution with phosphate buffer [59].
Hydrogels based on gelatin, xanthan gum, and cellulose obtained by reactive extrusion and thermopressing processes
Published in Preparative Biochemistry & Biotechnology, 2022
Jéssica F. Pereira, Beatriz M. Marim, Bruno M. Simões, Fabio Yamashita, Suzana Mali
Gelatin is a low-cost protein obtained from partial hydrolysis of collagen from skin, bones or connective tissue of animals, being classified as type A (acid hydrolysis) or type B gelatin (alkaline hydrolysis). Gelatin exhibits an amphoteric behavior due to the presence of both basic and acidic groups, presenting in its composition a large number of glycine, proline and hydroxyl-proline residues. It is widely used in food, cosmetic and pharmaceutical industries.[3,11] It is easily soluble in water at an average temperature of 40 °C, forming a viscous solution by chain association and three-dimensional network formation, resulting in gels and films employed for several applications.[11,12]
Preparation of Saccharomyces boulardii powder by spray drying: thermoprotectants optimization and stability evaluation
Published in Preparative Biochemistry & Biotechnology, 2022
Guowei Shu, Bohao Li, Chunji Dai, Li Chen, Xin Yang, Zhangteng Lei, Meng Zhang, Yuliang Guo
Gelatin is a denatured protein with agglutination effect, forming a thermoreversible gel in hot water, which has excellent water holding capacity. It prevents cell deformation and improves the heat resistance of bacteria.[37] Lian et al.[38] showed that by adding 10% (w/w) arabic gum, soluble starch or gelatin got the highest viability of Bifidobacteria by comparing different carrier concentrations. The viability of Bifidobacteria, which varies with the strain, depends largely on the type of carriers and concentration of carrier medium. According to Lian et al.,[38] the survival of Bifidobacteria decreased while the concentration of gelatin, soluble starch and arabic gum increased from 10% to 20% (w/w) or more.