Twenty-four Eastern Zhejiang White Geese were slaughtered, dry-cured by 2 different kinds of salt contents (12 geese with 4% low salt level [LS]; 12 geese with 8% high salt level [HS]) for one d, marinated in brine for one d, and air dry-ripened at 16 °C for 7 d. The effect of dry-curing salt contents on the changes in myofibril proteins, potential proteolysis activities, and total free amino acid (TFAA) in dry-cured goose was investigated. Compared to the raw, cathepsin B+L and calpains activities decreased at the end of dry-curing and the third d of dry-ripening. At the final products, the activities of cathepsin B+L and calpains were about half of those in raw meat. There was no difference in proteolysis activities except for the end of dry-curing (P < 0.05) and the 3 d of dry-ripening (P < 0.05) for cathepsin B+L, and the end of dry-curing (P < 0.05) for calpains (P < 0.05) between groups. Myosin light chain (MLC) and troponin-I were cleaved. Compared to the raw, TFAA increased by 36.64 and 31.82% in the final products for HS (P < 0.001) and LS (P < 0.01), respectively. The increase of TFAA could be attributed to the proteolysis of myofibril proteins and retained proteolysis activities. No significant difference on TFAA and MLC and troponin-I bands was observed between groups in final products. This means that different proteolysis activities during processing did not cause the difference in quality of final products between groups, and that 4% low salt can be used in future applications.