Sulfated fucan, an important marine polysaccharide frequently presented in echinoderms and brown algae, has gained growing attention owing to its various biological activities. Fucanases are essential tools for degrading sulfated fucan to produce corresponding oligosaccharides. In this context, an endo-1,3-fucanase (Fun187Al) belonging to the GH187 family was successfully expressed in Escherichia coli. Fun187Al showed the highest activity at temperatures of 30-40 °C and pH 7.5. It hydrolyzed sulfated fucans in a random endo-acting pattern, and displayed a substrate specificity different from the endo-1,3-fucanases of other glycoside hydrolase family. Analyses of ultra-performance liquid chromatography coupled with high-resolution mass spectrometry revealed that tetrasaccharide with two sulfate groups (Fuc