Lysozymes are important defense proteins of the innate immune system and possess high antibacterial activities. In the present study, a full-length c-type lysozyme cDNA (HtLysC) was cloned and characterized from taimen (Hucho taimen, Pallas). The cDNA contains an open reading frame (ORF) of 432 bp encoding 143 amino acid (aa), with 97% identity to LysC of Rainbow trout (Oncorhynchus mykiss). The amino acid sequence possessed a LYZ1 domain (16–140 aa) which contained two conserved residues (Glu 50 and Asp 67), eight conserved cysteine residues and a calcium binding site. RT-PCR analysis showed that HtLysC transcripts were most abundant in liver and less in muscle. The expression of HtLysC was up-regulated in the liver when challenged with Yersinia ruckeri. The recombinant HtLysC (rHtLysC) had lytic activities against Micrococcus lysodeikticus, Aeromonas salmonicida and Y. ruckeri. Enzyme assay showed that the optimal temperature and pH of rHtLysC were 55 °C and 6.0, respectively. Taken together, these results indicated that HtLysC might play an important role in innate immune defense against bacterial pathogens as a functional lysozyme.