agarase plays an important role in the enzymatic preparation of functional agaro-oligosaccharides. However, there are only few studies focused on α-agarases. An α-agarase named OUC-GaJJ96 from Gilvimarinus agarilyticus was cloned, and its enzymatic properties together with hydrolysis products were studied. OUC-GaJJ96 belong to glycoside hydrolase 96 family with a molecular weight of approximately 180 kDa. The gene OUC-GaJJ96 comprised a 3759bp, encoding a protein of 1252 amino acids, with a signal peptide of 26 amino acids at its N-terminal. The enzymatic properties of OUC-GaJJ96 showed that the optimal temperature and pH were 30℃ and 7.0 (Tris-HCl buffer), respectively. The specific activity of OUC-GaJJ96 was 2.68U/mg. The analysis of HPLC and ESI-MS demonstrated that the hydrolysis products of OUC-GaJJ96 were agarobiose, agarotetraose and agarohexaose, in which agarotetraose was the main product. Therefore, OUC-GaJJ96 has potential for the manufacture of bioactive agaro-oligosaccharides.