Thermal Stability of Chicken Keel Bone Collagen

Abstract

Acid‐soluble and pepsin‐solubilized collagen were isolated from chicken keel bone and analyzed by electrophoresis and circular dichroism. The denaturation temperature of chicken keel bone was determined by circular dichroism and compared to denaturation temperature of black drum or alligator bone. Our results show that collagen from chicken keel bone is a mixture of type II and type I, has predominantly the amino acids glycine, proline and hydroxyproline, and its secondary structure is predominantly triple‐helix. The onset of the denaturation temperature is 37C; at 44C, 50% of the collagen is denatured and the denaturation is complete at 48.8C making it the highest of vertebrate collagen denaturation temperatures reported in the literature. The high heat stability of chicken keel bone collagen may be in part ascribed to its imino acid content. Because of the high heat stability and low methionine content, chicken keel bone collagen is a high value‐added product with several biochemical and biomedical applications. Practical Applications The denaturation temperature of chicken keel bone collagen is above body temperature and allows applications in cosmetics where other types of collagen may be denatured because of their low denaturation temperature. Chicken type II collagen is well tolerated by patients with rheumatoid arthritis and is effective in the treatment of rheumatoid arthritis. Methionine‐restricted diet inhibits the growth of solid tumor such as gastric cancer, glioblastoma, medulloblastoma and neuroblastoma. Chicken type collagen may be a medical food for patients with solid tumors mentioned above.

Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

“…Glycine was the most abundant amino acid, accounting for 22.2% of the total, followed by alanine (10.2%), proline (9.5%), glutamic acid (9.4%) and hydroxyproline (5.8%), which were also present in the cartilage. Similar results were reported in the study of Losso & Dgawa (2014) when determining the amino acid composition of collagen extracted from chicken keel bone cartilage.…”

“…During processing of the chicken carcass, the filleting step generates a by-product known as keel bone cartilage, which is defined as a flexible cartilage that connects the breast muscle of the chicken to the tip of the sternum. This cartilage is discarded from the carcass after removal of the breast fillets (Losso & Dgawa, 2014). This cartilage is rich in collagen, which is a high added value product with possible biochemical and biomedical applications (Wang et al, 2017).…”

“…The composition of collagen from the cartilage of aquatic and terrestrial animals has been the object of study by researchers (Gómez-Guillén et al, 2011;Simões et al, 2014;Araújo et al, 2018) to identify bioactive compounds derived from cartilage with potential beneficial health properties. However, only one study published by Losso & Dgawa (2014) has focused on the extraction of collagen from chicken keel bone cartilage and its thermal stability. The present study aimed to optimize the effect of acid pretreatment, temperature and enzyme concentration on the acid-enzymatic extraction of soluble collagen from chicken keel bone cartilage.…”

Application of an antimicrobial packaging material from chicken bone gelatine and cinnamon bark oil to mozzarella cheese

“…We conclude that the composition of CBG is mostly similar to that of cattle bone gelatine, which also has high concentrations of Gly, Pro, Ala and Hyp (34.2%, 13.8%, 11.6% and 9.5%, respectively) (Avena‐Bustillos et al ., ). Our results regarding the amino acid composition of CBG are similar to those reported by Losso & Ogawa () for chicken keel bone gelatine.…”

Waste products from the poultry industry: a source of high‐value dietary supplements

“…17 It was found that the collagen from chicken keel cartilage is thermally stable and has a low methionine abundance, which enables its usage in several biochemical and biomedical applications. 19 Mechanically deboned chicken meat can also be used as a source of collagen, which was tested and described by Tanaka and Shimokomaki. 20 In both studies, the pepsin protease was used for the cartilage and tissues hydrolysis.…”