1Department of Veterinary Anatomy, Faculty of Veterinary and Animal Sciences, Banaras Hindu University, Barkachha, Mirzapur-231 001, Uttar Pradesh, India.
2Medical Laboratory Technology, DDU Kaushal Kendra, Banaras Hindu University, Barkachha, Mirzapur-231 001, Uttar Pradesh, India.
3Division of Livestock Products Technology, ICAR-Indian Veterinary Research Institute, Izatnagar, Bareilly-243 122, Uttar Pradesh, India.
4Teaching Veterinary Clinical Complex, Faculty of Veterinary and Animal Sciences, Banaras Hindu University, Barkachha, Mirzapur-231 001, Uttar Pradesh, India.
5Department of Veterinary Pathology, College of Veterinary Science and Animal Husbandry, NDVSU, Rewa-486 001, Madhya Pradesh, India.
6Department of Veterinary and Animal Husbandry Extension Education, College of Veterinary Science and Animal Husbandry, NDVSU, Rewa-486 001, Madhya Pradesh, India.
*Corresponding Author: Jigyasa Rana, Department of Veterinary Anatomy, Faculty of Veterinary and Animal Sciences, Banaras Hindu University, Barkachha, Mirzapur-231 001, Uttar Pradesh, India. Email: rana.jigyasa@gmail.com
Collagen is the most abundant protein found mainly in skin, bone, tendon and cartilage of animals and humans. Due to biocompatibility, biodegradability and minimal immunogenicity, collagen is extensively used in biomedical applications such as wound healing, tissue engineering and drug delivery systems. The study was aimed at extracting the collagen from chicken shank and evaluate it morphologically to ascertain its purity for biomedical application.
A total of 24, day-old broiler chicks were procured from commercial poultry farm located at Varanasi, Uttar Pradesh. The chicks were reared at Livestock Farm Complex, Faculty of Veterinary and Animal Sciences, RGSC, Banaras Hindu University. The chicks were divided into three groups of 8 birds each, viz. Group 1, Group 2 and Group 3 sacrificed for extraction of collagen from their shank at 28, 35 and 42 days respectively. Chicken shanks collected were cleaned, trimmed, peeled, deboned and ground for further extraction process. The ground material was subjected to pre-treatment by alkali and acid followed by enzymatic hydrolysis using pepsin enzyme. Thereafter, pre-treated tissue from shank was subjected to precipitation, centrifugation, dialysis and finally lyophilization for freeze drying. The yield of shank extracted collagen was recorded on wet weight basis and dry weight basis. The morphological characteristics of the extracted collagen were evaluated by Hematoxylin and Eosin (H and E) staining, Masson’s trichrome staining and electron microscopy.
The yield of extracted lyophilized collagen from group 1, 2 and 3 on dry weight basis is recorded as 0.132%, 0.182% and 0.215% respectively; whereas, the yield of extracted lyophilized collagen from group 1, 2 and 3 on wet weight basis was recorded as 0.130%, 0.181% and 0.213% respectively. The extracted collagen samples exhibited off-white colour with spongy paper-like consistency. Microscopically, the collagen from group 1 was found more fibrous with sheet-like structures, collagen from group 2 exhibited relatively less spongy admixture of sheet and little fibrillar structures; whereas, collagen from group 3 revealed dense fibrillar structure. The minimal basophilic content and clear background of H and E stained sections indicated purity of extracted collagen. The study successfully documented the extraction of high-quality collagen suitable for various biomedical applications. In addition, the study underlined the potential of utilizing low-value chicken by-products as a sustainable and cost-effective source of collagen, offering both environmental and economic benefits.
Collagen, Morphology, Poultry, Shank
