A novel GH16 β-porphyranase gene por16Z was cloned from marine bacterium Wenyingzhuangia aestuarii OF219 and expressed in E. coli， and the biochemical properties and hydrolytic patterns of the recombinant protein Por16Z_Wa were characterized. Por16Z_Wa showed the maximum activity at 45 ℃ and pH 6.5 and keep stable at a wide pH range from 4.0 to 9.0. Por16Z_Wa exhibited a cold-adapted property. Por16Z_Wa was an endo-acting enzyme. The final products of Por16Z_Wa were majorly composed of porphyran disaccharides L6S-G， with a minor portion of tetrasaccharides and hexasaccharides which were substituted by agarose moieties and (or) modified by methyl groups. Por16Z_Wa could be utilized as a promising tool for degradation of porphyran and directional preparation of porphyran disaccharides， which would facilitate the investigation of porphyran polysaccharides.