TECHNOLOGY FOCUS - ENVIRONMENT - Preferred Waste: The abalone process waste is gonad, esophagus, stomach, anus, mouth tissue, gill, gut, shell, head, frill, blood, meat or muscle tissue pieces. Preferred Abalone: The abalone is green-lip abalone (Haliotis laevigata), brown-lip abalone (Haliotis conicopora), Roe's abalone (Haliotis roei) and black-lip abalone (Haliotis ruber). EXAMPLE - Native collagen was extracted from the individual parts of the muscle tissue using acetic acid. The presence, quantity and quality of collagen from the different parts of the abalone muscle were determined. The abalone muscle was divided into foot (pedal sole), the dorsal surface of foot (epipodium), and adductor (columellar) muscle. The foot and adductor muscle were further separated into soft and hard parts, and upper and middle parts, respectively. Pigments were removed from the tissue, various muscle parts (A = 4 g, B = 28 g, C = 7 g, D = 47 g and E = 3 g) were dissected, cut into smaller pieces and treated separately. 0.5 M acetic acid solution (pH 3) was added to the tissue. The individual suspensions (A = 150 ml, B = 100 ml, C = 50 ml, D = 200 ml and E = 200 ml) were stirred overnight. Part D was not stirred and allowed to stand overnight. The supernatant (Dasterisk) was retained for analysis to determine if collagen was extracted without any agitation to the tissue. A further 200 ml of 0.5 M acetic acid was added to the remaining part D tissue. The suspensions were homogenized. The pH of the slurry was adjusted to 3.5 with a small volume of 1 N HCl. The slurry was stirred overnight to extract collagen fibrils. The solution was centrifuged at 3000 rpm, for 20 minutes to remove tissue particulates. In order to precipitate the native collagen fibrils the supernatant was brought to 0.3 M sodium chloride by gradually adding solid sodium chloride to the supernatant with constant stirring. Visible white collagen fibrils precipitated within 2 minutes. The solution was allowed to stir overnight to further extract the native collagen fibrils. The solution had a high viscosity indicating the presence of collagen. The native collagen fibrils were collected by centrifugation at 5000 rpm, at 4 degrees C for 30 minutes. The native collagen fibrils from parts A, B, C, D, Dasterisk and E were each dissolved in a minimum quantity of de-ionized water. The native collagen fibrils were extensively dialyzed against de-ionized water to remove any salt. The native collagen fibrils from parts A, B, C, D, Dasterisk, and E were transferred into separate freeze drying bottles and frozen in liquid nitrogen. The samples were freeze dried for 16 hours. The freeze dried native abalone collagen fibrils A, B, C, D exhibited white and spongy fibers, Dasterisk exhibited cream, rubbery fibers, and E exhibited white and crisp fibers. The native abalone collagen fibril showed extraction yield of 10 % of A, 7.1 % of B, 91 % of C, 3.1 % of D, 6.8 % of Dasterisk and 60 % of E. Sample A, B, C, D, Dasterisk, E had protein concentration of 0.430, 0.449, 0.428, 0.421, 0.073 and 0.636 mg/ml, respectively. The sample A, B, C, D and E showed clear solution appearance and Dasterisk showed large amount of settled and suspended material.