Collagen packets
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Collagen Packets: Enhancing Structure-Stability and Packaging Characteristics
Introduction to Collagen-Based Films
Collagen, a protein widely used in the food industry, has shown potential for creating edible packaging films. However, its inherent thermal instability and mechanical weaknesses limit its broader application. Recent research has focused on improving these properties by crosslinking collagen with other proteins and compounds.
Crosslinking with Casein, Keratin, and Soy Protein Isolate
Improved Thermal Stability and Mechanical Properties
Crosslinking collagen with proteins such as casein, keratin, and soy protein isolate (SPI) using transglutaminase (TGase) has been shown to significantly enhance its thermal stability and mechanical properties. The formation of higher molecular weight complexes and larger particle sizes in the protein mixture, especially after TGase crosslinking, contributes to these improvements. Differential scanning calorimetry (DSC) analysis revealed that collagen-casein complexes exhibit superior thermal stability compared to other combinations.
Enhanced Packing Characteristics
The addition of casein, keratin, and SPI to collagen fiber-based films results in better packing characteristics, including improved barrier properties, mechanical strength, and thermal stability. Specifically, films with 500 g/kg casein demonstrated the highest thermal stability, while those with 100 g/kg casein showed the greatest tensile strength. Films with 100 g/kg keratin exhibited the highest elongation-at-break values, indicating better flexibility.
Blending with Sodium Alginate, Starch, and Sodium Carboxymethyl Cellulose
Formation of a Homogeneous Network Structure
Collagen extracted from pig skin and blended with sodium alginate, starch, and sodium carboxymethyl cellulose, followed by crosslinking with glutaraldehyde, forms a strong hydrogen-bonded network. This network structure significantly enhances the mechanical properties of the films, such as elongation at break and tensile strength. The addition of sodium alginate, in particular, improves the interaction between molecules, resulting in a more homogeneous surface morphology.
Conclusion
The crosslinking of collagen with proteins like casein, keratin, and SPI, as well as blending with compounds such as sodium alginate, starch, and sodium carboxymethyl cellulose, significantly enhances the thermal stability, mechanical properties, and packing characteristics of collagen-based films. These advancements could promote the broader application of collagen in food packaging, offering a promising solution for creating more stable and durable edible films.
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