The use of regenerative medicine is on an all-time high resulting in a huge demand for renewable, biodegradable and biocompatible biomaterials. Collagen comprises 30% of the mammalian body’s protein, being the main component of skin, connective tissue and cartilage. Bovine hides are a by-product of the meat industry and contain a significant amount of collagen. In this study the methods of acid-solubilisation (AS), acid-enzyme solubilisation (AES1) and a modified acid-enzyme solubilisation (AES2) were carried out to for comparative purposes to extract collagen from bull, calf, cow, face-piece and ox-hides. Acid solubilisation aids in removal of acidic proteins due to weakening of interactions between the acidic proteins and collagen fibrils, whereas acid-enzyme solubilisation maximises the extraction process by the action of proteolytic enzyme pepsin cleaving to the natural cross-linking sites of collagen (telopeptides). Purification was carried out by repetitive precipitation and dialysis. By AS extraction, collagen dry yields of 2.3-25.4% were obtained with highest yield being from calf hide. AES1 resulted in collagen dry yields of 18.2-31.3%, with bull hide resulting in the highest dry yield. Collagen dry yields ranged between 20.6-40.1% with AES2 extraction method. Hydroxyproline analysis resulted in collagen contents of 1.3-10.6% by one-stage purification with the method of AS extraction. However AS extraction with three-stage purification resulted in collagen contents of 3.8-25.7%. Collagen contents of 8.2-12.6% were obtained by AES1 extraction method with one-stage purification and 15.4-30.2% with three-stage purification. AES2 resulted in collagen contents of 23.95-35.99% with one-stage purification and 48.9-74.5% with three-stage purification which was significantly higher than found in recent literature. All the collagen samples revealed were type I with α, β, and γ chains as indicated by SDS-PAGE pattern.