ArticleRSC advances2020
Characterization of biocompatible pig skin collagen and application of collagen-based films for enzyme immobilization.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Enzymatic Production of Collagen Oligopeptides from Porcine Skin and Their Structure-Activity Relationships in Anti-Aging and Skin-Whitening Effect.Foods (Basel, Switzerland) · 2026Article
- Comparative analysis of collagen from different sources for wound and burn management.Biomaterials translational · 2026Article
- Strategies for the Implementation of Chenodeoxycholic Acid in Natural Polymer-Based Hydrogels for Stable and Low-Light Effective Quasi-Solid Electrolytes for Aqueous Dye-Sensitized Solar Cells.ACS applied energy materials · 2025Article
- Progress in Research on Animal Collagen Peptides: Preparation, Bioactivity, and Application.Molecules (Basel, Switzerland) · 2025Review
- Unveiling the Potential of Protein-Based Sustainable Antibacterial Materials.Probiotics and antimicrobial proteins · 2025Review
- Exploring the Possibilities of Using Recovered Collagen for Contaminants Removal-A Sustainable Approach for Wastewater Treatment.Polymers · 2024Review
- Creation of Chemically Tri-Layered Collagen Crosslinked Membranes and Their Comparison with Ionically Tri-Layered Chitosan Crosslinked Membranes to Study Human Skin Properties.International journal of molecular sciences · 2023Article
- Collagen Extraction from Animal Skin.Biology · 2022Review
- A new iron supplement: The chelate of pig skin collagen peptide and FeFrontiers in nutrition · 2022Article
- Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection.Molecular pharmaceutics · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on the excellent biocompatibility of collagen, collagen was extracted from pig skin by acid-enzymatic method. The films were prepared by the self-aggregation behavior of collagen, and the catalase was immobilized by adsorption, cross-linking and embedding. The experiment investigated the effects of glutaraldehyde on the mechanical properties, external sensory properties, and denaturation temperature of the films. The results showed that self-aggregating material could maintain the triple helix structure of pig skin collagen. The self-aggregation treatment and cross-linking treatment can improve the mechanical properties to 53 MPa, while the glutaraldehyde cross-linking agent can increase the denaturation temperature of the pig skin collagen self-aggregating membrane by 20.35% to 84.48 °C. This means that its application to immobilized catalase has better stability. The comparison shows that the catalase immobilized by the adsorption method has strong activity and high operational stability, and the cross-linking agent glutaraldehyde and the initial enzyme concentration have a significant effect on the immobilization, and the activity can reach 175 U g
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Registered trials
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