Extraction and characterization of collagen with or without telopeptides from chicken skin

Abstract

Poultry by-products are not often processed into high-value products. Rather than being transformed into meal for animal feed, a large quantity of chicken skin could be used to produce collagen, which is valued for its unique functional properties. The purpose of this research project was to extract and characterize collagen from chicken skin. Skins were first ground and then were heated to 40 or 60 degrees C to extract the fat. After mechanical separation, the collagen contained in the resulting solid phase was extracted with pepsin or ethylene diamine. Types I and III collagen were then isolated and characterized by SDS PAGE, antigen labeling, determination of tyrosine residues, and transmission electron microscopy. The total collagen content of the skin was recovered from the solid phase following heat treatment at 40 degrees C. Extraction yields varied with the solubilization process: 38.9% of the collagen content in the solid phase was extracted with pepsin and 25.1% with ethylene diamine. Ratios of type I to type III collagen fractionated using NaCl were 74.4:19.8% with pepsin and 62.4:31.7% with ethylene diamine. Characterization tests further revealed the presence of telopeptides solely on ethylene diamine-solubilized collagen. Chicken skin thus appears to be a good alternative source of high-quality collagen.

Effects of Soaking pH and Extracting Temperature on the Physicochemical Properties of Chicken Skin Gelatin

“…Abedin and Riemschneider (1984) reported that chicken skin contains 75% type I collagen and 15% type III collagen. Similarly, Cliche et al (2003) reported that chicken skin collagen treated with pepsin or ethylene diamine contains two α chains and the migration patterns of two treatments were similar. In addition, Shin (2002) found that the collagen in chicken feet was comprised of α 1 and α 2 chains.…”

“…Chicken skin which contains approximate 3% collagen has also been identified as a potential novel collagen source (Bonifer and Froning, 1996). Cliche et al (2003) reported that the collagen extracted from chicken skin is comprised of about 75% type I collagen and 15% type III collagen. Extraction methods of collagen from chicken skin involve acetic acid and pepsin treatment (Bannister and Burns, 1972) and pepsin or ethylene diamine extraction after mechanical separation (Cliche et al, 2003).…”

“…Cliche et al (2003) reported that the collagen extracted from chicken skin is comprised of about 75% type I collagen and 15% type III collagen. Extraction methods of collagen from chicken skin involve acetic acid and pepsin treatment (Bannister and Burns, 1972) and pepsin or ethylene diamine extraction after mechanical separation (Cliche et al, 2003). Gelatin derived from the collagen through (Kim et al, 1988).…”

The influence of chicken scratch collagen with local hydroxyapatite as bone substitute material toward the bone remodelling of Rattus Sprague Dawley

“…Chicken scratch extract containing 38.6% type 1 collagen fibers are composed of amino acids for the synthesis of collagen fibers. [17] Benefits of this research are new information for the development of science in the Dentistry Prosthodontics in particular. The alternative materials product for rehabilitation of bone is chicken scratch collagen with local hydroxyapatite as a bone substitute material.…”

“…The extraction of skin chicken scratch contains 38,6% collagen. [16] Extracts of chicken scratch collagen is extracted from the skin of chicken scratch at 60°C will produce 38,6% collagen content [17] On the forming process of bone basic matrix in the form of a collagens matrix by the activity of osteoblasts and fibroblasts, there was calcification of the new bone tissue. [18] Chicken scratch collagen has no cytotoxicity on fibroblast cell.…”