Abstract

Syeda Tashrufa Nashfin, Md. Awlad Hossain Babu*, Shuvo Ranjan Das

ABSTRACT

Background: Collagen is the predominant structural protein in animals, constituting roughly 30% of total protein in mammals. It serves an essential function in the extracellular matrix, offering structural stability to skin, tendons, cartilage, and connective tissues. (Shoulders & Raines, 2009). In the food sector, collagen and its derivatives—especially gelatin and collagen hydrolysates—are valued for their functional properties, including gelling, emulsification, water retention, and nutritional benefits. (Silva et al., 2014). Cattle skins are a significant by-product of the leather and meat industries. Significant quantities of raw hide and trimmings are frequently discarded or underutilized, leading to waste management and environmental issues. Utilizing bovine hide for collagen extraction not only enhances its economic value but also promotes sustainability by minimizing waste. (Schmidt et al., 2016). The study aimed to produce cowhide collagen and apply it to food product development. This study employed two different extraction methods for cowhide: an acid and alkali combined synthesis method and an alkaline synthesis method. The observed parameters consisted of yield, moisture, ash, pH, protein, emulsifying, and gel strength tests. The result showed the difference in the pre-extraction process. Collagen has unique characteristics that make it widely applicable in food products. Methodology: All experiments were performed in the Process and Analytical Lab Department of Food Engineering and Technology at the State University of Bangladesh. Protein tests were performed in the WAFFEN Research Lab. In my experiments, the chemicals used without further purification were calcium hydroxide and acetic acid. Cow hides were collected from the local market. The procedure involved measuring the unprocessed material (cowhide). Additionally, the hide was soaked in water at 70 °C for 15 minutes to prepare it for the unhairing process. The hairs on the hide were then taken off using a manual method. The initial process involved weighing raw material (cowhide). The sample, in fresh condition and clean (without hair), was cut into a rectangle measuring 2 cm x 3 cm. A total of 4 beakers were prepared for the treatment containers of T1, T2, T3, and T4. Ca(OH)2 and CH3COOH solutions were each inserted into the beaker glass. 100 g of cowhide as raw material was divided into four pieces of beaker glass and soaked for 4 days at room temperature. The hide sample was then removed from the beaker and washed with running water. These samples were further extracted in a water bath at 70 °C for 24 hours. The extraction results were then filtered to produce a filtrate of liquid collagen extract. The result was dried in an oven at 60 °C for 24 hours to produce a dry collagen extract, and then packed in airtight glass jars. (Said, 2018). Result: A study was conducted on the extraction of collagen from cow hide. Collagen extract from cow hide was obtained by using the extraction and characterization of extracted collagen, yielding samples (1, 2, 3, 4). Yield is (11.20, 11.60, 6.70, 5.50) %. After analyzing the collagen, I found the moisture content to be (S1 = 7.8%, S2 = 7.2%, S3 = 6.8%, S4 = 6.7%). The ash content which is (S1= 1.4%, S2=1.55%, S3=1.75%. S4= 1.9%). The protein content was 77.51% and 41.02% in the collagen. Sample (1, 2, 3, 4) moisture content is (7.8%, 7.2%, 6.8%, 6.7%). Ash is (1.4, 1.55, 1.75, 1.90) %. PH is (8.90, 8.10, 7.50, 6.64), Protein is (77.51, Nil, Nil, 41.02) %. TDS (PPM) is (109, 117, 120, Nil), Stability (Hours) is (14, 12, 09, Nil). This Collagen shows strong gelatinizing properties. This Collagen shows strong emulsifying strength.