Abstract
Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.
Highlights
Collagen is the most important protein produced by the human body, it is mainly formed by the amino acid glycine (33%), proline and hydroxyproline (22%) in a triplex helix which is formed by three α chains
Hydrolyzed collagen (HC) can be extracted from different sources and tissues [71], it can be extracted from bovine Achilles tendon by using different enzymes such as alcalase, pepsin, trypsin, and collagenase produced by Penicillium aurantiogriseum
HC has a wide range of applications due to its properties such as: low viscosity in aqueous solutions, neutral odor, colorlessness, transparency, emulsification and stabilization, foam forming, film forming, wettability, solubility, dispersibility, powder compressibility, substance carrier of low allergenicity as well as antioxidant and antimicrobial activity
Summary
Collagen is the most important protein produced by the human body, it is mainly formed by the amino acid glycine (33%), proline and hydroxyproline (22%) (primary structure) in a triplex helix which is formed by three α chains. Collagen extraction can be carried out from different tissues such as bones, tendons, lung tissue, or even connective tissue [18,19,20,21] Extraction under acid treatment is usually applied for extraction of collagen type I from tissues of porcine or fish skin origin [34]. The use of ultrasound as an alternative method for collagen extraction does not change the molecule and facilitates the enzymatic action This technology can be applied in different tissues such as fish skin and bovine tendons in order to produce higher collagen concentrations in shorter extraction times [38,39,40]. Pre-treatment conditions, dialysis, and source of extraction are the main factors that determine final collagen characteristics such as molecular weight, amino acid composition, and molecular structure [41,42]
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