Cross-Industry Application of Gelatin from Food Industry to Biomedicine
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Cross-Industry Application of Gelatin from Food Industry to Biomedicine

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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
ACM9000708-10Gelatin from bovine skin, BioreagantInquiry
ACM9000708-11Gelatin from fish skinInquiry
ACM9000708-12Gelatin from porcine skin, BioreagantInquiry
ACM9000708-13Gelatin solutionInquiry
ACM9000708-14Gelatin, 130 Bloom, 3.2 mPa.sInquiry
ACM9000708-15Gelatin, 140-160 Bloom, 2.5-3.5 mPa.sInquiry
ACM9000708-16Gelatin, 140-170 Bloom, 3.0-4.3 mPa.sInquiry
ACM9000708-17Gelatin, 140-180 Bloom, 2.8-3.6 mPa.sInquiry
ACM9000708-18Gelatin, 150 Bloom, 4.0 mPa.sInquiry
ACM9000708-19Gelatin, 150-180 Bloom, 3.3-4.3 mPa.sInquiry
ACM9000708-20Gelatin, 160-190 Bloom, 3.5-4.3 mPa.sInquiry
ACM9000708-21Gelatin, 170-195 Bloom (67 mg/ml water)Inquiry
ACM9000708-22Gelatin, 180 Bloom, 4.4 mPa.sInquiry
ACM9000708-23Gelatin, 180-220 Bloom, 2.8-3.6 mPa.sInquiry
ACM9000708-24Gelatin, 190-210 Bloom, 2.4-3.4 mPa.sInquiry
ACM9000708-25Gelatin, 190-210 Bloom, 2.8-3.5 mPa.sInquiry
ACM9000708-26Gelatin, 200 Bloom, 4.6 mPa.sInquiry
ACM9000708-27Gelatin, 210-230 Bloom, 2.8-3.5 mPa.sInquiry
ACM9000708-28Gelatin, 210-260 Bloom, 4.0-5.0 mPa.sInquiry
ACM9000708-29Gelatin, 220 Bloom, 4.7 mPa.sInquiry
ACM9000708-30Gelatin, 240 Bloom, 4.9 mPa.sInquiry
ACM9000708-31Gelatin, 240-260 Bloom, 3.0-4.0 mPa.sInquiry
ACM9000708-32Gelatin, 250 Bloom, 4.0-5.0 mPa.sInquiry
ACM9000708-33Gelatin, 260-330 Bloom, 4.0-6.5 mPa.sInquiry
ACM9000708-34Gelatin, 40-50% in H2O, ~60 kDaInquiry
ACM9000708-35Gelatin, 80-120 Bloom, 1.8-2.8 mPa.sInquiry
ACM9000708-36Gelatin, 90-110 Bloom, 2.0-3.0 mPa.sInquiry
ACM9000708-37Gelatin, Microbiological GradeInquiry
ACM9000708-38Gelatin, Pharmaceutical GradeInquiry
ACM9000708-39Gelatin, Photographic GradeInquiry
ACM9000708-40Gelatin, Type A, 240-270 BloomInquiry
ACM9000708-4Low endotoxin gelatin from porcine skinInquiry
ACM9000708-41Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-30: 30±5%Inquiry
ACM9000708-42Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-60: 60±5%Inquiry
ACM9000708-43Green fluorescently labeled methacrylated gelatin, double bond modification degree GM-90: 90±5%Inquiry
ACM9000708-44High porosity methacrylated gelatin, Porosity: 30-40%Inquiry
ACM9000708-45High porosity methacrylated gelatin, Porosity: 50-60%Inquiry
ACM9000708-46Low endotoxin gelatin from bovine boneInquiry
ACM9000708-47Low endotoxin non-gelling gelatin from porcine skinInquiry
ACM9000708-48Methacrylated Gelatin, Grafting Rate:17%Inquiry
ACM9000708-49Methacrylated Gelatin, Grafting Rate:30%Inquiry
ACM9000708-50Methacrylated Gelatin, Grafting Rate:60%Inquiry
ACM9000708-51Methacrylated Gelatin, Grafting Rate:90%Inquiry
ACM9000708-52Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-30: 30±5%Inquiry
ACM9000708-53Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-60: 60±5%Inquiry
ACM9000708-54Red fluorescently labeled methacrylated gelatin, double bond modification degree GM-90: 90±5%Inquiry
ACM9000708-55Allyl-modified gelatin, gel strength : 300 BloomInquiry
ACM9000708-56mPEG functionalized gelatin, 50% PEGylationInquiry

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. Overview of the application of gelatin in various fields.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

  1. Alipal, J., et al. Materials Today: Proceedings, 2021, 42, 240-250.
  2. Xiang, Lei, et al. Journal of Leather Science and Engineering, 2021, 3, 1-24.
  3. Jia, Xiaoyu, et al. Biomacromolecules, 2024, 25(2), 564-589.
  4. Waidi, Yusuf Olatunji, et al. Frontiers in Bioengineering and Biotechnology, 2024, 12, 1357460.

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