Laminaribiose in food and health: biological functions, applications, and recent advances in enzymatic production via green multi-enzyme cascade synthesis

Laminaribiose, a β-1,3-linked glucose disaccharide, possesses notable bioactivities with potential applications in food and health. Its industrial use is constrained by low yield and purity. Production strategies include natural extraction, chemical synthesis, and enzymatic synthesis. Natural extraction preserves bioactivity but is inefficient, chemical synthesis affords structural control but suffers from byproducts and toxicity, whereas enzymatic synthesis offers mild, efficient catalysis with improved yield. Enzymatic synthesis of laminaribiose has been established through systems ranging from single to multi-enzyme cascades. Single-enzyme approaches employ β-glucosidase or β-1,3-glucanase, while dual-enzyme systems use sucrose phosphorylase (SP) and laminaribiose phosphorylase (LBP) with sucrose and glucose. Tri-enzyme systems of α-glucan phosphorylase (αGP), α-glucosidase (αG), and LBP utilize starch. In contrast, four-enzyme cascades integrate αGP, LBP, isoamylase (IA), and 4-α-glucanotransferase (4GT) with maltodextrin and glucose, or combine cellobiohydrolase I (CBHI), cellodextrin phosphorylase (CDP), cellobiose phosphorylase (CBP), and LBP with cellulose. Advances in enzyme engineering, particularly for LBP, have further enhanced catalytic efficiency. This review critically summarizes recent advances in the biological functions, applications, and enzymatic synthesis of laminaribiose, with particular focus on multi-enzyme cascade strategies and their catalytic features. It aims to provide a conceptual framework for developing efficient, sustainable synthesis and advancing industrial applications.