Alginate lyases show great potential for industrial and medicinal applications, especially as an attractive biocatalyst for the production of oligosaccharides with special bioactivities. A novel alginate lyase, AlyH1, from the marine bacterium Vibrio furnissii H1, which has been newly isolated from rotten seaweed, was purified and characterized. The purified enzyme showed the specific activity of 2.40 U/mg. Its molecular mass was 35.8 kDa. The optimal temperature and pH were 40 °C and pH 7.5, respectively. AlyH1 maintained stability at neutral pH (7.0–8.0) and temperatures below 30 °C. Metal ions Na⁺, Mg²⁺, and K⁺ increased the activity of the enzyme. With sodium alginate as the substrate, the Km and Vmax values of AlyH1 were 2.28 mg/mL and 2.81 U/mg, respectively. AlyH1 exhibited activities towards both polyguluronate and polymannuronate, and preferentially degraded polyguluronate. Products prepared from sodium alginate by AlyH1 were displayed to be di-, tri-, and tetra-alginate oligosaccharides. A partial amino acid sequence (190 aa) of AlyH1 analysis suggested that AlyH1 was an alginate lyase of polysaccharide lyase family 7. The sequence showed less than 77% identity to the reported alginate lyases. These data demonstrated that AlyH1 could be as a novel and potential candidate in application of alginate oligosaccharides production with low polymerization degrees.

In recent years, polymeric hydrogels have appeared promising matrices for enzyme immobilization to design, signify and expand bio-catalysis engineering. Therefore, the development and deployment of polymeric supports in the form of hydrogels and other robust geometries are continuously growing to green the twenty-first-century bio-catalysis. Furthermore, adequately fabricated polymeric hydrogel materials offer numerous advantages that shield pristine enzymes from denaturation under harsh reaction environments. For instance, cross-linking modulation of hydrogels, distinct rheological behavior, tunable surface entities along with elasticity and mesh size, larger surface-volume area, and hydrogels’ mechanical cushioning attributes are of supreme interest makes them the ideal candidate for enzyme immobilization. Furthermore, suitable coordination of polymeric hydrogels with requisite enzyme fraction enables pronounced loading, elevated biocatalytic activity, and exceptional stability. Additionally, the unique catalytic harmony of enzyme-loaded polymeric hydrogels offers numerous applications, such as hydrogels as immobilization matrix, bio-catalysis, sensing, detection and monitoring, tissue engineering, wound healing, and drug delivery applications. In this review, we spotlight the applied perspective of enzyme-loaded polymeric hydrogels with recent and relevant examples. The work also signifies the combined use of multienzyme systems and the future directions that should be attempted in this field.