Mannanase with a molecular weight of 33.1 kDa was purified from Weissella cibaria F1. The F1 mannanase contained 289 amino acid residues and shared 70.0% similarity with mannanase from Bacillus subtilis (P55278 (MANB_BACIU)). The optimum reaction conditions of F1 mannanase were 50 °C and pH 6.5. After incubation at pH 4.5–8.0 and 30–60 °C for 2 h, the enzyme activity remained above 60%. The effects of metal ions on mannanase enzyme activity were measured, and Mn2+, Mg2+, and Cu2+ increased

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... e activity. The Km (16.96 ± 0.01 μmol·mL−1) and Vmax (1119.05 ± 0.14 μmol·min−1) values showed that the enzyme exhibited high affinity for locust bean gum. Mannanase was used to hydrolyze konjac glucomannan to produce konjac oligo-glucomannan (KOGM). KOGM increased the proliferation and phagocytosis of RAW264.7 macrophages and enhanced nitric oxide, and cytokine production in macrophages, which showed potent immunostimulatory activity. In this study, the advantages of mannanase derived from lactic acid bacteria were utilized to expand the application of KOGM in the medical field, which is helpful to explore the broad prospects of KOGM in functional food or medicine.