As a major component of the extracellular matrix, collagen has been used as a biomaterial for many purposes including tissue engineering. Commercial collagen derived from mammals is associated with a risk of prion diseases and religious restrictions, while fish-derived collagen can avoid such issues. In addition, fish-derived collagen is widely available and low-cost; however, it often suffers from poor thermal stability, which limits its biomedical application. In this study, collagen with a high thermal stability was successfully extracted from the swim bladder of silver carp (Hypophthalmichthys molitrix) (SCC). The results demonstrated that it was a type I collagen with high purity and well-preserved triple-helix structure. Amino acid composition assay showed that the amounts of threonine, methionine, isoleucine and phenylalanine in the collagen of swim bladder of silver carp were higher than those of bovine pericardium. After adding salt solution, swim-bladder-derived collagen could form fine and dense collagen fibers. In particular, SCC exhibited a higher thermal denaturation temperature (40.08 °C) compared with collagens from the swim bladder of grass carp (Ctenopharyngodon idellus) (GCC, 34.40 °C), bovine pericardium (BPC, 34.47 °C) and mouse tail (MTC, 37.11 °C). Furthermore, SCC also showed DPPH radical scavenging ability and reducing power. These results indicate that SCC presents a promising alternative source of mammalian collagen for pharmaceutical and biomedical applications.