Cloning, Expressing and Characterizing a Novel Cold-Adapted Laminarinase from Marine Bacterium Wenyingzhuangia aestuarii OF219

Laminarinases reveal potential application in the field of food and biotechnology. In this research, a novel GH16 family laminarinase, designated as Lam16A_Wa, was cloned from the genome of marine bacterium Wenyingzhuangia aestuarii OF219 and expressed in Escherichia coli . Lam16A_Wa demonstrates a relatively low optimal reaction temperature (35°C) and a cold-adapted feature. Its optimal pH value is 6.0 and is stable in a broad pH range from 3.0 to 11.0. A glycomics strategy was employed to investigate the hydrolytic pattern of Lam16A_Wa. The enzyme was confirmed as a random endo-acting glycoside hydrolase. Its minimum substrate was laminarin pentasaccharide, and the major final products are oligosaccharides, including disaccharide to pentasaccharide. The Lam16A_Wa provides a novel and well-defined tool for the molecular tailoring of laminarin.