Dbtaining collagen and hydrolysates from mechanically separated chicken meat residue is an excellent way to add value to this waste. The aims of this study were to obtain collagen hydrolysates from chicken MSM residue using Alcalase  and Flavourzyme  enzymes, as well characterizing the functional, structural and thermal stability properties. The highest degree of hydrolysis was obtained using Alcalase  , 36.11%, while using Flavourzyme  resulted in 12.02%. The DSC analysis of the collagen indicated a denaturation temperature of 46.47 °C. The FTOR spectra of the crude collagen showed absorption peaks that were characteristic of amide bands A, B, O, OO and OOO. On the spectra of the hydrolysed the area of the amide bands was reduced, and some peaks appeared between 800 and 1,200 cm-1. The disappearance of high molecular weight bands in the SDS-PAGE analysis also confirmed the hydrolysis of collagen. After the hydrolysis, the collagen presented reduced viscosity, the capacity to form foam, and foam stability. The emulsifying activity index was high in the hydrolysates in relation to the crude collagen. Thus, the use of Alcalase  and Flavourzyme  to obtain hydrolysates from collagen derived from chicken MSM residue was shown to be viable, and potentially useful for industrial applications.