Bovine hide collagen peptides
Pro Research Analysisby 
Searched over 200M research papers
Bovine Hide Collagen Peptides: Production, Properties, and Applications
Enzymatic Production of Bovine Hide Collagen Peptides
Modification of Porcine Pepsin for Gelatin Production
The enzymatic production of bovine hide collagen peptides can be optimized by modifying the substrate specificity of enzymes like porcine pepsin. Through site-directed mutagenesis, researchers have altered porcine pepsin to selectively cleave bovine hide collagen at specific sites, similar to cathepsin D. This modification enhances the solubilization rate of bovine hide collagen while maintaining the triple helix structure, thus minimizing denaturation and proteolytic cleavage.
Recombinant Collagenase from Bacillus cereus
Another approach involves using recombinant bacterial collagenase from Bacillus cereus to hydrolyze bovine bone collagen into collagen-soluble peptides (CPP). This method not only increases the added value of bovine bone byproducts but also produces peptides with significant antioxidant activities, making them suitable for functional food applications.
Characterization and Bioactivity of Collagen Peptides
Cyanogen Bromide Peptides
Cyanogen bromide digestion of bovine collagen yields various peptides, which can be characterized using electrophoresis. These peptides, derived from both soluble and insoluble collagens, show tissue-specific cross-linking patterns and contain unique sequences that contribute to their bioactivity .
Antioxidant and Moisture-Retention Properties
Collagen peptides derived from bovine sources exhibit notable antioxidant properties. For instance, peptides produced using thermolysin-like protease A69 from Anoxybacillus caldiproteolyticus show high hydroxyl radical scavenging activity and moisture-retention ability, indicating their potential use in cosmetics and food industries. Additionally, peptides-minerals complexes from bovine bone have demonstrated significant antioxidant activity, which can be enhanced by optimizing enzyme-collagen ratios and processing conditions.
Health Benefits and Functional Applications
Skin Aging and Fibroblast Growth
Oral administration of collagen peptides from bovine bone has been shown to improve skin laxity and collagen content in chronologically aged mice. These peptides also enhance antioxidative enzyme activities in the skin, suggesting their potential as functional foods to combat skin aging. Furthermore, specific collagen-derived peptides like Prolyl-Hydroxyproline (Pro-Hyp) and Hydroxyprolyl-Glycine (Hyp-Gly) have been found to promote fibroblast growth, which is crucial for skin and joint health.
Food and Pharmaceutical Applications
The versatility of collagen peptides extends to various applications in the food and pharmaceutical industries. They can act as natural emulsifiers, foaming agents, and biodegradable film-forming materials. The enzymatic hydrolysis of collagen not only produces bioactive peptides with antimicrobial, antioxidant, and antihypertensive properties but also ensures excellent absorption and metabolism in the body.
Conclusion
Bovine hide collagen peptides, produced through various enzymatic processes, exhibit significant bioactive properties, including antioxidant activity and skin health benefits. These peptides hold great potential for applications in functional foods, cosmetics, and pharmaceuticals, contributing to the valorization of bovine byproducts and promoting sustainable practices in the agro-food industry.
Sources and full results
Most relevant research papers on this topic