During leather processing, raw skins/hides are trimmed and thrown as wastes and accountingrnfor pollution load in leather industry. Elastin is a fibrous protein with multifaceted applicationsrnin biomedical field due to its intrinsic biological annotations viz elasticity and cell interactions,rnthe extraction process is challenging task due to their cell interactive properties, the applicationrnis versatile and the price is in current international market is highly expensive. In this context,rnleather solid wastes specifically raw hide trimmings have been found out in the research as thernpotential source of raw material for elastin extraction. In this research, the raw Hide Trimmingrnelastin content was estimated between in the range of 122 mAUmin and 97 mAUmin using therncombination of FPLC, UV-Spectroscopy, SDS-PAGE protein scientific characterizationrntechniques. The Elastin was extracted from leather waste through autoclaving technology, thernmethod yield was found to be 90%. In addition, the biocompatibility study confirms that there isrnno toxic nature of extracted elastin for biological application. This implies that the selectedrnextraction process was effective and efficient. The physical characterization using DSC resultrnindicates that the melting peak of elastin was -0.5420 watt/g at 103.23 rnC, elastin showed veryrnhigh denaturation temperature of 275.82rnornC and TGA studies confirm that elastin have six massrnloss degradation steps. The chemical characterization result using rnornC Solid state NMR andrnFTIR that elastin shows random coil, Î±-helix and Î²-strand secondary structure. Moreover, thernFTIR confirm that amide A, I, II, III, IV, V, VI, and VII functional group existed in the elastinrnfiber. The biological characterization using amino acid analysis result show that the amino acidrncomposition chain of the product have high amount of glycine, non-polar amino acid, lowrnamount of acidic amino acids, low amount of hydroxyl amino acid and there is no hydroxylsine,rntryptophan and Cysteine amino acids in the amino acid composition of the protein fiber. Thernlittle variations were the existence of high amount of basic amino acids in the protein amino acidrncomposition due to the presence of collagen residues. Finally, the biocompatibility study showsrnthat there is no toxicity nature of the extracted elastin fiber for human keratinocyte cells culture.rnThere result is scientifically justified and confirmed that the raw hide trimmings extracted elastinrnmakes feasible for biological and biomedical applications.