Chicken collagen casings could be an alternate source of collagen casings that are manufactured for sausages. The overall objective of this project was to extract chicken collagen from by-products of the broiler processing industries and to explore the possibility of making films. Chicken skin was washed, ground, and pretreated to remove the noncollagenous compounds. Collagen was extracted using acetic acid and pepsin. Solubilized collagen was salted-out and centrifuged at 20,000 ×g at 4°C for one hour. The precipitates were dissolved in 0.5 M acetic acid and dialyzed against 0.1 M acetic acid and distilled water before freeze-drying. Molecular weight, collagen solubility at different pH values, and NaCl concentrations were determined. TA-XT2 texture analyzer was used to characterize mechanical properties of collagen films. The highest collagen solubility was obtained at pH 2 and 2% NaCl. Hand-homogenized, nonfiltered, and conditioned samples had the highest hardness (3,262 g) and the least brittleness (30.5 mm). These results demonstrate that chicken collagen extracted from chicken by-products has the ability to form films and could be considered for making casings or be used in various other industries.