Gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad (SMG) were obtained by enzymatic hydrolysis using neutrase. Functional properties of SMG hydrolysates (SMGHs) with different degree of hydrolysis (DH: 4.94, 6.84, 7.53 and 11.86%, respectively) were evaluated with the objective to investigate the relations between hydrolysis characteristics and functionalities. The results showed that hydrolysis with neutrase improved the gelation property, solubility, waterholding capacity (WHC), oil-holding capacity (OHC), and surface hydrophobicity (SH), but not foaming capacity (FC) of SMG. The SMGHs at high DH (11.86%) showed better gelation property and solubility than that at low DH (4.94-7.53%). However, the maximum values of WHC, OHC, and SH of SMGHs were found at DH of 4.94%, significantly higher than (p \ 0.05) or equivalent to (p [ 0.05) that of soy protein isolate (SPI) for WHC and OHC. Emulsifying capacity of SMGHs is independent of DH, but restricted by pH environment. The emulsifying activity index of all SMGHs was significantly higher than that of SPI in pH 5 (p \ 0.05) and slightly higher than or equivalent to that of SPI in pH 7. Meanwhile, SMG and SMGHs were abundant in glycine, lysine, alanine, glutamic acid, and aspartic acid, containing all the essential amino acids (41.63-42.90% of the total amino acids). These results imply that SMGHs might be utilized as multifunctional and nutritive ingredients in food industry.