Gelatin is a protein derived from collagen, typically found in the skin, bones, and connective tissues of animals. It is a versatile ingredient widely used in the food, pharmaceutical, and cosmetic industries for its gelling, thickening, and stabilizing properties. Gelatin is a translucent, colorless, and tasteless substance that can be formed into a gel or used as a thickening agent.
Characteristics of Gelatin
Gelatin is a water-soluble protein with distinctive properties that make it a valuable ingredient in various products. Its unique characteristics include gelling ability, film-forming capability, emulsifying properties, and the ability to stabilize foams. These properties are directly related to the structure of gelatin, which is primarily composed of amino acids, including high amounts of glycine, proline, and hydroxyproline. The presence of these amino acids imparts gelatin with its gelling and film-forming properties. Furthermore, gelatin exhibits excellent binding capabilities, making it an ideal ingredient for thickening, stabilizing, and texturizing food and pharmaceutical products.
Source and Extraction of Gelatin
Gelatin is traditionally derived from animal sources such as pig skin, bovine hides, and bones. In the industry, pig skin and pig bones or cow skin are considered to be type A gelatin, and type B gelatin is usually extracted from beef raw materials and sometimes from pig bones. The commonly used acid and alkali agents used in industry to extract minerals and bacteria from these raw materials are caustic lime or sodium carbonate. In general, taking pig and cattle-based gelatin as an example, the typical production process involves:
- Degreasing: soaking in hot water after washing, and then baking at 100°C for at least 30 minutes to reduce about 2% of fat.
- Pretreatment: soaking in acid (quicklime, usually 4% hydrochloric acid, HCl pH < 1.5) or alkali (potassium carbonate or sodium carbonate, Na2CO3 pH > 7) barrels for about 5 days. Acid pretreatment yields type A gelatin, while alkaline hydrolysis yields type B gelatin.
- Extraction: Load into an extractor and boil in distilled water, then rapidly heat the resulting liquid gelatin to around 140°C in 4 seconds for sterilization.
- Evaporation: The liquid is piped through a filter to separate any bone, tissue or skin fragments still attached. The filtered liquid is piped into an evaporator to separate the liquid from the solid gelatin.
- Grinding: The solid gelatin is pressed into flakes and then ground into a fine powder (sweeteners, flavorings and coloring agents can be added at this point).
Gelatins from Alfa Chemistry
Catalog | Product Name | Price |
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ACM9000708-10 | Gelatin from bovine skin, Bioreagant | Inquiry |
ACM9000708-11 | Gelatin from fish skin | Inquiry |
ACM9000708-12 | Gelatin from porcine skin, Bioreagant | Inquiry |
ACM9000708-13 | Gelatin solution | Inquiry |
ACM9000708-14 | Gelatin, 130 Bloom, 3.2 mPa.s | Inquiry |
ACM9000708-15 | Gelatin, 140-160 Bloom, 2.5-3.5 mPa.s | Inquiry |
ACM9000708-16 | Gelatin, 140-170 Bloom, 3.0-4.3 mPa.s | Inquiry |
ACM9000708-17 | Gelatin, 140-180 Bloom, 2.8-3.6 mPa.s | Inquiry |
ACM9000708-18 | Gelatin, 150 Bloom, 4.0 mPa.s | Inquiry |
ACM9000708-19 | Gelatin, 150-180 Bloom, 3.3-4.3 mPa.s | Inquiry |
ACM9000708-20 | Gelatin, 160-190 Bloom, 3.5-4.3 mPa.s | Inquiry |
ACM9000708-21 | Gelatin, 170-195 Bloom (67 mg/ml water) | Inquiry |
ACM9000708-22 | Gelatin, 180 Bloom, 4.4 mPa.s | Inquiry |
ACM9000708-23 | Gelatin, 180-220 Bloom, 2.8-3.6 mPa.s | Inquiry |
ACM9000708-24 | Gelatin, 190-210 Bloom, 2.4-3.4 mPa.s | Inquiry |
ACM9000708-25 | Gelatin, 190-210 Bloom, 2.8-3.5 mPa.s | Inquiry |
ACM9000708-26 | Gelatin, 200 Bloom, 4.6 mPa.s | Inquiry |
ACM9000708-27 | Gelatin, 210-230 Bloom, 2.8-3.5 mPa.s | Inquiry |
ACM9000708-28 | Gelatin, 210-260 Bloom, 4.0-5.0 mPa.s | Inquiry |
ACM9000708-29 | Gelatin, 220 Bloom, 4.7 mPa.s | Inquiry |
ACM9000708-30 | Gelatin, 240 Bloom, 4.9 mPa.s | Inquiry |
ACM9000708-31 | Gelatin, 240-260 Bloom, 3.0-4.0 mPa.s | Inquiry |
ACM9000708-32 | Gelatin, 250 Bloom, 4.0-5.0 mPa.s | Inquiry |
ACM9000708-33 | Gelatin, 260-330 Bloom, 4.0-6.5 mPa.s | Inquiry |
ACM9000708-34 | Gelatin, 40-50% in H2O, ~60 kDa | Inquiry |
ACM9000708-35 | Gelatin, 80-120 Bloom, 1.8-2.8 mPa.s | Inquiry |
ACM9000708-36 | Gelatin, 90-110 Bloom, 2.0-3.0 mPa.s | Inquiry |
ACM9000708-37 | Gelatin, Microbiological Grade | Inquiry |
ACM9000708-38 | Gelatin, Pharmaceutical Grade | Inquiry |
ACM9000708-39 | Gelatin, Photographic Grade | Inquiry |
ACM9000708-40 | Gelatin, Type A, 240-270 Bloom | Inquiry |
ACM9000708-4 | Low endotoxin gelatin from porcine skin | Inquiry |
ACM9000708-41 | Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-30: 30±5% | Inquiry |
ACM9000708-42 | Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-60: 60±5% | Inquiry |
ACM9000708-43 | Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-90: 90±5% | Inquiry |
ACM9000708-44 | High porosity methacrylated gelatin, Porosity: 30-40% | Inquiry |
ACM9000708-45 | High porosity methacrylated gelatin, Porosity: 50-60% | Inquiry |
ACM9000708-46 | Low endotoxin gelatin from bovine bone | Inquiry |
ACM9000708-47 | Low endotoxin non-gelling gelatin from porcine skin | Inquiry |
ACM9000708-48 | Methacrylated Gelatin, Grafting Rate:17% | Inquiry |
ACM9000708-49 | Methacrylated Gelatin, Grafting Rate:30% | Inquiry |
ACM9000708-50 | Methacrylated Gelatin, Grafting Rate:60% | Inquiry |
ACM9000708-51 | Methacrylated Gelatin, Grafting Rate:90% | Inquiry |
ACM9000708-52 | Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-30: 30±5% | Inquiry |
ACM9000708-53 | Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-60: 60±5% | Inquiry |
ACM9000708-54 | Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-90: 90±5% | Inquiry |
ACM9000708-55 | Allyl-modified gelatin, gel strength : 300 Bloom | Inquiry |
ACM9000708-56 | mPEG functionalized gelatin, 50% PEGylation | Inquiry |
Gelatin in Biomedical Applications
The applications of gelatin are wide and varied, involving multiple industries such as food, cosmetics, and biomedicine. In the food industry, gelatin is used as a gelling agent in candies, dairy products, and meat products. In addition, gelatin is widely used in cosmetics due to its film-forming and emulsifying properties. Its unique properties, such as biocompatibility, biodegradability, and ease of functionalization, make it highly attractive for various biomedical applications. Below we focus on the application and progress of gelatin in biomedicine.
Fig 1. Various applications of gelatin. [1]
Gelatin in Tissue Engineering
In tissue engineering, gelatin serves as a fundamental component due to its ability to mimic the extracellular matrix, promoting cell adhesion, growth, and differentiation. Gelatin-based hydrogels have been extensively studied for tissue regeneration applications, including wound healing, bone regeneration, and cartilage repair. These hydrogels provide a supportive environment for cell proliferation and tissue formation, making them ideal scaffolds for tissue engineering.[2]
Gelatin in Drug Delivery Systems
Gelatin-based nanoparticles, microparticles, and hydrogels have been developed for targeted drug delivery, controlled release, and enhanced therapeutic efficacy. These systems offer advantages such as biocompatibility, tunable mechanical properties, and the ability to encapsulate a wide range of therapeutic agents. Gelatin-based drug delivery systems have shown potential in treating various diseases, including cancer, infections, and chronic wounds. [3]
Gelatin in 3D Bioprinting
Gelatin-based bioinks are commonly used in bioprinting due to their printability, biocompatibility, and ability to support cell growth and differentiation. These bio-printed structures find applications in regenerative medicine, organ-on-a-chip models, and personalized medicine, showcasing the versatility of gelatin in shaping the future of tissue engineering. [4]
References
- Alipal, J., et al. Materials Today: Proceedings, 2021, 42, 240-250.
- Xiang, Lei, et al. Journal of Leather Science and Engineering, 2021, 3, 1-24.
- Jia, Xiaoyu, et al. Biomacromolecules, 2024, 25(2), 564-589.
- Waidi, Yusuf Olatunji, et al. Frontiers in Bioengineering and Biotechnology, 2024, 12, 1357460.
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